{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,14]],"date-time":"2026-08-14T00:25:15Z","timestamp":1786667115232,"version":"build-2736575974"},"reference-count":55,"publisher":"Springer Science and Business Media LLC","issue":"1","license":[{"start":{"date-parts":[[2019,10,10]],"date-time":"2019-10-10T00:00:00Z","timestamp":1570665600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0"},{"start":{"date-parts":[[2019,10,10]],"date-time":"2019-10-10T00:00:00Z","timestamp":1570665600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0"}],"funder":[{"DOI":"10.13039\/501100004359","name":"Vetenskapsr\u00e5det","doi-asserted-by":"publisher","award":["2016-06264"],"award-info":[{"award-number":["2016-06264"]}],"id":[{"id":"10.13039\/501100004359","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100004359","name":"Vetenskapsr\u00e5det","doi-asserted-by":"publisher","award":["2017-03827"],"award-info":[{"award-number":["2017-03827"]}],"id":[{"id":"10.13039\/501100004359","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Sci Rep"],"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Pathogens often receive antibiotic resistance genes through horizontal gene transfer from bacteria that produce natural antibiotics. ErmE is a methyltransferase (MTase) from <jats:italic>Saccharopolyspora erythraea<\/jats:italic> that dimethylates A2058 in 23S rRNA using S-adenosyl methionine (SAM) as methyl donor, protecting the ribosomes from macrolide binding. To gain insights into the mechanism of macrolide resistance, the crystal structure of ErmE was determined to 1.75\u2009\u00c5 resolution. ErmE consists of an N-terminal Rossmann-like \u03b1\/\u00df catalytic domain and a C-terminal helical domain. Comparison with ErmC\u2019 that despite only 24% sequence identity has the same function, reveals highly similar catalytic domains. Accordingly, superposition with the catalytic domain of ErmC\u2019 in complex with SAM suggests that the cofactor binding site is conserved. The two structures mainly differ in the C-terminal domain, which in ErmE contains a longer loop harboring an additional 3<jats:sub>10<\/jats:sub> helix that interacts with the catalytic domain to stabilize the tertiary structure. Notably, ErmE also differs from ErmC\u2019 by having long disordered extensions at its N- and C-termini. A C-terminal disordered region rich in arginine and glycine is also a present in two other MTases, PikR1 and PikR2, which share about 30% sequence identity with ErmE and methylate the same nucleotide in 23S rRNA.<\/jats:p>","DOI":"10.1038\/s41598-019-51174-0","type":"journal-article","created":{"date-parts":[[2019,10,10]],"date-time":"2019-10-10T10:40:39Z","timestamp":1570704039000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":24,"title":["Crystal structure of ErmE - 23S rRNA methyltransferase in macrolide resistance"],"prefix":"10.1038","volume":"9","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-6560-011X","authenticated-orcid":false,"given":"Alena","family":"Stsiapanava","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9079-2774","authenticated-orcid":false,"given":"Maria","family":"Selmer","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2019,10,10]]},"reference":[{"key":"51174_CR1","doi-asserted-by":"crossref","first-page":"203","DOI":"10.1146\/annurev-biochem-113009-092313","volume":"82","author":"RM Voorhees","year":"2013","unstructured":"Voorhees, R. M. & Ramakrishnan, V. Structural basis of the translational elongation cycle. Annu. Rev. Biochem. 82, 203\u2013236 (2013).","journal-title":"Annu. Rev. Biochem."},{"key":"51174_CR2","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1038\/nrmicro3155","volume":"12","author":"DN Wilson","year":"2014","unstructured":"Wilson, D. N. Ribosome-targeting antibiotics and mechanisms of bacterial resistance. Nat. Rev. Microbiol. 12, 35\u201348 (2014).","journal-title":"Nat. Rev. Microbiol."},{"key":"51174_CR3","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1146\/annurev-micro-090817-062329","volume":"72","author":"N V\u00e1zquez-Laslop","year":"2018","unstructured":"V\u00e1zquez-Laslop, N. & Mankin, A. S. Context-Specific Action of Ribosomal Antibiotics. Annu. Rev. Microbiol. 72, 185\u2013207 (2018).","journal-title":"Annu. Rev. Microbiol."},{"key":"51174_CR4","doi-asserted-by":"crossref","first-page":"879","DOI":"10.1016\/0300-9084(87)90215-X","volume":"69","author":"D Moazed","year":"1987","unstructured":"Moazed, D. & Noller, H. F. Chloramphenicol, erythromycin, carbomycin and vernamycin B protect overlapping sites in the peptidyl transferase region of 23S ribosomal RNA. Biochimie 69, 879\u2013884 (1987).","journal-title":"Biochimie"},{"key":"51174_CR5","doi-asserted-by":"crossref","first-page":"949","DOI":"10.2174\/1568026033452159","volume":"3","author":"M Gaynor","year":"2003","unstructured":"Gaynor, M. & Mankin, A. S. Macrolide antibiotics: binding site, mechanism of action, resistance. Curr. Top. Med. Chem. 3, 949\u2013961 (2003).","journal-title":"Curr. Top. Med. Chem."},{"key":"51174_CR6","doi-asserted-by":"crossref","first-page":"12702","DOI":"10.1016\/S0021-9258(17)44232-3","volume":"258","author":"R Skinner","year":"1983","unstructured":"Skinner, R., Cundliffe, E. & Schmidt, F. J. Site of action of a ribosomal RNA methylase responsible for resistance to erythromycin and other antibiotics. J. Biol. Chem. 258, 12702\u201312706 (1983).","journal-title":"J. Biol. Chem."},{"key":"51174_CR7","doi-asserted-by":"crossref","first-page":"453","DOI":"10.1007\/s00284-002-3901-8","volume":"46","author":"WS Champney","year":"2003","unstructured":"Champney, W. S., Chittum, H. S. & Tober, C. L. A 50S ribosomal subunit precursor particle is a substrate for the ErmC methyltransferase in Staphylococcus aureus cells. Curr. Microbiol. 46, 453\u2013460 (2003).","journal-title":"Curr. Microbiol."},{"key":"51174_CR8","doi-asserted-by":"crossref","first-page":"147","DOI":"10.4161\/rna.4.3.5346","volume":"4","author":"I Pokkunuri","year":"2007","unstructured":"Pokkunuri, I. & Champney, W. S. Characteristics of a 50S ribosomal subunit precursor particle as a substrate for ermE methyltransferase activity and erythromycin binding in Staphylococcus aureus. RNA Biol. 4, 147\u2013153 (2007).","journal-title":"RNA Biol."},{"key":"51174_CR9","doi-asserted-by":"crossref","first-page":"207","DOI":"10.1146\/annurev.mi.43.100189.001231","volume":"43","author":"E Cundliffe","year":"1989","unstructured":"Cundliffe, E. How antibiotic-producing organisms avoid suicide. Annu. Rev. Microbiol. 43, 207\u2013233 (1989).","journal-title":"Annu. Rev. Microbiol."},{"key":"51174_CR10","first-page":"281","volume":"2","author":"JM McGUIRE","year":"1952","unstructured":"McGUIRE, J. M. et al. Ilotycin, a new antibiotic. Antibiot. Chemother. 2, 281\u2013283 (1952).","journal-title":"Antibiot. Chemother."},{"key":"51174_CR11","doi-asserted-by":"crossref","first-page":"447","DOI":"10.1038\/nbt1297","volume":"25","author":"M Oliynyk","year":"2007","unstructured":"Oliynyk, M. et al. Complete genome sequence of the erythromycin-producing bacterium Saccharopolyspora erythraea NRRL23338. Nat. Biotechnol. 25, 447\u2013453 (2007).","journal-title":"Nat. Biotechnol."},{"key":"51174_CR12","doi-asserted-by":"crossref","first-page":"1464","DOI":"10.1128\/jb.137.3.1464-1467.1979","volume":"137","author":"MY Graham","year":"1979","unstructured":"Graham, M. Y. & Weisblum, B. 23S ribosomal ribonucleic acid of macrolide-producing streptomycetes contains methylated adenine. J. Bacteriol. 137, 1464\u20131467 (1979).","journal-title":"J. Bacteriol."},{"key":"51174_CR13","doi-asserted-by":"crossref","first-page":"85","DOI":"10.1093\/jac\/40.1.85","volume":"40","author":"A Bonnefoy","year":"1997","unstructured":"Bonnefoy, A., Girard, A. M., Agouridas, C. & Chantot, J. F. Ketolides lack inducibility properties of MLS(B) resistance phenotype. J. Antimicrob. Chemother. 40, 85\u201390 (1997).","journal-title":"J. Antimicrob. Chemother."},{"key":"51174_CR14","doi-asserted-by":"crossref","first-page":"122","DOI":"10.1111\/j.1749-6632.2011.06323.x","volume":"1241","author":"JA Sutcliffe","year":"2011","unstructured":"Sutcliffe, J. A. Antibiotics in development targeting protein synthesis. Ann. N. Y. Acad. Sci. 1241, 122\u2013152 (2011).","journal-title":"Ann. N. Y. Acad. Sci."},{"key":"51174_CR15","doi-asserted-by":"crossref","first-page":"138","DOI":"10.1007\/BF00638597","volume":"37","author":"H Brockman","year":"1950","unstructured":"Brockman, H. & Henkel, W. Pikromycin, ein neues Antibiotikumaus Actinomyceten. Naturwissenschaften 37, 138\u2013139 (1950).","journal-title":"Naturwissenschaften"},{"key":"51174_CR16","doi-asserted-by":"crossref","first-page":"12956","DOI":"10.1073\/pnas.1512090112","volume":"112","author":"MM Almutairi","year":"2015","unstructured":"Almutairi, M. M. et al. Resistance to ketolide antibiotics by coordinated expression of rRNA methyltransferases in a bacterial producer of natural ketolides. Proc. Natl. Acad. Sci. USA 112, 12956\u201312961 (2015).","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"51174_CR17","doi-asserted-by":"crossref","first-page":"2212","DOI":"10.1038\/nprot.2007.321","volume":"2","author":"FH Niesen","year":"2007","unstructured":"Niesen, F. H., Berglund, H. & Vedadi, M. The use of differential scanning fluorimetry to detect ligand interactions that promote protein stability. Nat. Protoc. 2, 2212\u20132221 (2007).","journal-title":"Nat. Protoc."},{"key":"51174_CR18","doi-asserted-by":"crossref","first-page":"012001","DOI":"10.1088\/1742-6596\/425\/1\/012001","volume":"425","author":"P Theveneau","year":"2013","unstructured":"Theveneau, P. et al. The Upgrade Programme for the Structural Biology beamlines at the European Synchrotron Radiation Facility \u2013 High throughput sample evaluation and automation. J. Phys. Conf. Ser. 425, 012001 (2013).","journal-title":"J. Phys. Conf. Ser."},{"key":"51174_CR19","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1107\/S0907444909047337","volume":"66","author":"W Kabsch","year":"2010","unstructured":"Kabsch, W. XDS. Acta Crystallogr. D Biol. Crystallogr. 66, 125\u2013132 (2010).","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"51174_CR20","doi-asserted-by":"crossref","first-page":"658","DOI":"10.1107\/S0021889807021206","volume":"40","author":"AJ McCoy","year":"2007","unstructured":"McCoy, A. J. et al. Phaser crystallographic software. J. Appl. Crystallogr. 40, 658\u2013674 (2007).","journal-title":"J. Appl. Crystallogr."},{"key":"51174_CR21","doi-asserted-by":"crossref","first-page":"277","DOI":"10.1006\/jmbi.1999.2788","volume":"289","author":"G Schluckebier","year":"1999","unstructured":"Schluckebier, G., Zhong, P., Stewart, K. D., Kavanaugh, T. J. & Abad-Zapatero, C. The 2.2 A structure of the rRNA methyltransferase ErmC\u2019 and its complexes with cofactor and cofactor analogs: implications for the reaction mechanism. J. Mol. Biol. 289, 277\u2013291 (1999).","journal-title":"J. Mol. Biol."},{"key":"51174_CR22","doi-asserted-by":"crossref","first-page":"271","DOI":"10.1016\/j.jmb.2009.02.066","volume":"388","author":"H Demirci","year":"2009","unstructured":"Demirci, H. et al. Structural rearrangements in the active site of the Thermus thermophilus 16S rRNA methyltransferase KsgA in a binary complex with 5\u2032-methylthioadenosine. J. Mol. Biol. 388, 271\u2013282 (2009).","journal-title":"J. Mol. Biol."},{"key":"51174_CR23","doi-asserted-by":"crossref","first-page":"483","DOI":"10.1038\/nsb0697-483","volume":"4","author":"L Yu","year":"1997","unstructured":"Yu, L. et al. Solution structure of an rRNA methyltransferase (ErmAM) that confers macrolide-lincosamide-streptogramin antibiotic resistance. Nat. Struct. Biol. 4, 483\u2013489 (1997).","journal-title":"Nat. Struct. Biol."},{"key":"51174_CR24","doi-asserted-by":"crossref","first-page":"884","DOI":"10.1016\/j.jmb.2009.06.015","volume":"391","author":"N Pulicherla","year":"2009","unstructured":"Pulicherla, N. et al. Structural and functional divergence within the Dim1\/KsgA family of rRNA methyltransferases. J. Mol. Biol. 391, 884\u2013893 (2009).","journal-title":"J. Mol. Biol."},{"key":"51174_CR25","doi-asserted-by":"crossref","first-page":"167","DOI":"10.1107\/S2059798318003455","volume":"74","author":"RM Keegan","year":"2018","unstructured":"Keegan, R. M. et al. Recent developments in MrBUMP: better search-model preparation, graphical interaction with search models, and solution improvement and assessment. Acta Crystallogr D Struct Biol 74, 167\u2013182 (2018).","journal-title":"Acta Crystallogr D Struct Biol"},{"key":"51174_CR26","doi-asserted-by":"crossref","first-page":"61","DOI":"10.1107\/S090744490705024X","volume":"64","author":"TC Terwilliger","year":"2008","unstructured":"Terwilliger, T. C. et al. Iterative model building, structure refinement and density modification with the PHENIX AutoBuild wizard. Acta Crystallogr. D Biol. Crystallogr. 64, 61\u201369 (2008).","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"51174_CR27","doi-asserted-by":"crossref","first-page":"1171","DOI":"10.1038\/nprot.2008.91","volume":"3","author":"G Langer","year":"2008","unstructured":"Langer, G., Cohen, S. X., Lamzin, V. S. & Perrakis, A. Automated macromolecular model building for X-ray crystallography using ARP\/wARP version 7. Nat. Protoc. 3, 1171\u20131179 (2008).","journal-title":"Nat. Protoc."},{"key":"51174_CR28","doi-asserted-by":"crossref","first-page":"486","DOI":"10.1107\/S0907444910007493","volume":"66","author":"P Emsley","year":"2010","unstructured":"Emsley, P., Lohkamp, B., Scott, W. G. & Cowtan, K. Features and development of Coot. Acta Crystallogr. D Biol. Crystallogr. 66, 486\u2013501 (2010).","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"51174_CR29","doi-asserted-by":"crossref","first-page":"352","DOI":"10.1107\/S0907444912001308","volume":"68","author":"PV Afonine","year":"2012","unstructured":"Afonine, P. V. et al. Towards automated crystallographic structure refinement with phenix.refine. Acta Crystallogr. D Biol. Crystallogr. 68, 352\u2013367 (2012).","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"51174_CR30","doi-asserted-by":"crossref","first-page":"12","DOI":"10.1107\/S0907444909042073","volume":"66","author":"VB Chen","year":"2010","unstructured":"Chen, V. B. et al. MolProbity: all-atom structure validation for macromolecular crystallography. Acta Crystallogr. D Biol. Crystallogr. 66, 12\u201321 (2010).","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"51174_CR31","unstructured":"The PyMOL Molecular Graphics System, Version 2.3 Schr\u00f6dinger, LLC."},{"key":"51174_CR32","doi-asserted-by":"crossref","first-page":"W460","DOI":"10.1093\/nar\/gkm363","volume":"35","author":"T Ishida","year":"2007","unstructured":"Ishida, T. & Kinoshita, K. PrDOS: prediction of disordered protein regions from amino acid sequence. Nucleic Acids Res. 35, W460\u20134 (2007).","journal-title":"Nucleic Acids Res."},{"key":"51174_CR33","doi-asserted-by":"crossref","first-page":"774","DOI":"10.1016\/j.jmb.2007.05.022","volume":"372","author":"E Krissinel","year":"2007","unstructured":"Krissinel, E. & Henrick, K. Inference of macromolecular assemblies from crystalline state. J. Mol. Biol. 372, 774\u2013797 (2007).","journal-title":"J. Mol. Biol."},{"key":"51174_CR34","doi-asserted-by":"crossref","first-page":"W351","DOI":"10.1093\/nar\/gkw357","volume":"44","author":"L Holm","year":"2016","unstructured":"Holm, L. & Laakso, L. M. Dali server update. Nucleic Acids Res. 44, W351\u20135 (2016).","journal-title":"Nucleic Acids Res."},{"key":"51174_CR35","doi-asserted-by":"crossref","first-page":"194","DOI":"10.1038\/250194a0","volume":"250","author":"MG Rossmann","year":"1974","unstructured":"Rossmann, M. G., Moras, D. & Olsen, K. W. Chemical and biological evolution of nucleotide-binding protein. Nature 250, 194\u2013199 (1974).","journal-title":"Nature"},{"key":"51174_CR36","doi-asserted-by":"crossref","first-page":"3784","DOI":"10.1093\/nar\/29.18.3784","volume":"29","author":"X Cheng","year":"2001","unstructured":"Cheng, X. & Roberts, R. J. AdoMet-dependent methylation, DNA methyltransferases and base flipping. Nucleic Acids Res. 29, 3784\u20133795 (2001).","journal-title":"Nucleic Acids Res."},{"key":"51174_CR37","doi-asserted-by":"crossref","first-page":"7103","DOI":"10.1021\/bi973113c","volume":"37","author":"DE Bussiere","year":"1998","unstructured":"Bussiere, D. E. et al. Crystal structure of ErmC\u2019, an rRNA methyltransferase which mediates antibiotic resistance in bacteria. Biochemistry 37, 7103\u20137112 (1998).","journal-title":"Biochemistry"},{"key":"51174_CR38","doi-asserted-by":"crossref","first-page":"4941","DOI":"10.1093\/nar\/gkg666","volume":"31","author":"G Maravi\u0107","year":"2003","unstructured":"Maravi\u0107, G., Bujnicki, J. M., Feder, M., Pongor, S. & Fl\u00f6gel, M. Alanine-scanning mutagenesis of the predicted rRNA-binding domain of ErmC\u2019 redefines the substrate-binding site and suggests a model for protein-RNA interactions. Nucleic Acids Res. 31, 4941\u20134949 (2003).","journal-title":"Nucleic Acids Res."},{"key":"51174_CR39","doi-asserted-by":"crossref","first-page":"W469","DOI":"10.1093\/nar\/gkq406","volume":"38","author":"MN Wass","year":"2010","unstructured":"Wass, M. N., Kelley, L. A. & Sternberg, M. J. E. 3DLigandSite: predicting ligand-binding sites using similar structures. Nucleic Acids Res. 38, W469\u201373 (2010).","journal-title":"Nucleic Acids Res."},{"key":"51174_CR40","doi-asserted-by":"crossref","first-page":"618","DOI":"10.1006\/jmbi.1995.0577","volume":"253","author":"T Malone","year":"1995","unstructured":"Malone, T., Blumenthal, R. M. & Cheng, X. Structure-guided analysis reveals nine sequence motifs conserved among DNA amino-methyltransferases, and suggests a catalytic mechanism for these enzymes. J. Mol. Biol. 253, 618\u2013632 (1995).","journal-title":"J. Mol. Biol."},{"key":"51174_CR41","doi-asserted-by":"crossref","first-page":"D200","DOI":"10.1093\/nar\/gkw1129","volume":"45","author":"A Marchler-Bauer","year":"2017","unstructured":"Marchler-Bauer, A. et al. CDD\/SPARCLE: functional classification of proteins via subfamily domain architectures. Nucleic Acids Res. 45, D200\u2013D203 (2017).","journal-title":"Nucleic Acids Res."},{"key":"51174_CR42","doi-asserted-by":"crossref","first-page":"D427","DOI":"10.1093\/nar\/gky995","volume":"47","author":"S El-Gebali","year":"2019","unstructured":"El-Gebali, S. et al. The Pfam protein families database in 2019. Nucleic Acids Res. 47, D427\u2013D432 (2019).","journal-title":"Nucleic Acids Res."},{"key":"51174_CR43","doi-asserted-by":"crossref","first-page":"337","DOI":"10.1016\/j.jmb.2004.02.068","volume":"339","author":"HC O\u2019Farrell","year":"2004","unstructured":"O\u2019Farrell, H. C., Scarsdale, J. N. & Rife, J. P. Crystal structure of KsgA, a universally conserved rRNA adenine dimethyltransferase in Escherichia coli. J. Mol. Biol. 339, 337\u2013353 (2004).","journal-title":"J. Mol. Biol."},{"key":"51174_CR44","doi-asserted-by":"crossref","first-page":"9537","DOI":"10.1093\/nar\/gkt719","volume":"41","author":"AS Punekar","year":"2013","unstructured":"Punekar, A. S., Liljeruhm, J., Shepherd, T. R., Forster, A. C. & Selmer, M. Structural and functional insights into the molecular mechanism of rRNA m6A methyltransferase Rlm. J. Nucleic Acids Res. 41, 9537\u20139548 (2013).","journal-title":"J. Nucleic Acids Res."},{"key":"51174_CR45","doi-asserted-by":"crossref","first-page":"575","DOI":"10.1038\/nature18298","volume":"534","author":"X Wang","year":"2016","unstructured":"Wang, X. et al. Structural basis of N6-adenosine methylation by the METTL3\u2013METTL14 complex. Nature 534, 575 (2016).","journal-title":"Nature"},{"key":"51174_CR46","doi-asserted-by":"crossref","first-page":"986","DOI":"10.1016\/j.molcel.2018.08.004","volume":"71","author":"M Mendel","year":"2018","unstructured":"Mendel, M. et al. Methylation of Structured RNA by the m6A Writer METTL16 Is Essential for Mouse Embryonic Development. Mol. Cell 71, 986\u20131000.e11 (2018).","journal-title":"Mol. Cell"},{"key":"51174_CR47","doi-asserted-by":"crossref","first-page":"1001","DOI":"10.1016\/j.molcel.2018.07.025","volume":"71","author":"KA Doxtader","year":"2018","unstructured":"Doxtader, K. A. et al. Structural Basis for Regulation of METTL16, an S-Adenosylmethionine Homeostasis Factor. Mol. Cell 71, 1001\u20131011.e4 (2018).","journal-title":"Mol. Cell"},{"key":"51174_CR48","doi-asserted-by":"crossref","DOI":"10.1038\/s41598-018-23608-8","volume":"8","author":"A Ruszkowska","year":"2018","unstructured":"Ruszkowska, A., Ruszkowski, M., Dauter, Z. & Brown, J. A. Structural insights into the RNA methyltransferase domain of METTL16. Sci. Rep. 8, 5311 (2018).","journal-title":"Sci. Rep."},{"key":"51174_CR49","doi-asserted-by":"crossref","first-page":"10453","DOI":"10.1074\/jbc.M111.318121","volume":"287","author":"D Boehringer","year":"2012","unstructured":"Boehringer, D., O\u2019Farrell, H. C., Rife, J. P. & Ban, N. Structural insights into methyltransferase KsgA function in 30S ribosomal subunit biogenesis. J. Biol. Chem. 287, 10453\u201310459 (2012).","journal-title":"J. Biol. Chem."},{"key":"51174_CR50","doi-asserted-by":"crossref","first-page":"374","DOI":"10.1016\/j.str.2009.01.010","volume":"17","author":"C Tu","year":"2009","unstructured":"Tu, C. et al. Structural basis for binding of RNA and cofactor by a KsgA methyltransferase. Structure 17, 374\u2013385 (2009).","journal-title":"Structure"},{"key":"51174_CR51","doi-asserted-by":"crossref","first-page":"255","DOI":"10.1006\/jmbi.1998.2024","volume":"282","author":"B Vester","year":"1998","unstructured":"Vester, B., Nielsen, A. K., Hansen, L. H. & Douthwaite, S. ErmE methyltransferase recognition elements in RNA substrates. J. Mol. Biol. 282, 255\u2013264 (1998).","journal-title":"J. Mol. Biol."},{"key":"51174_CR52","doi-asserted-by":"crossref","first-page":"1425","DOI":"10.1021\/jacs.8b10277","volume":"141","author":"R Bhujbalrao","year":"2019","unstructured":"Bhujbalrao, R. & Anand, R. Deciphering Determinants in Ribosomal Methyltransferases That Confer Antimicrobial Resistance. J. Am. Chem. Soc. 141, 1425\u20131429 (2019).","journal-title":"J. Am. Chem. Soc."},{"key":"51174_CR53","doi-asserted-by":"crossref","first-page":"W604","DOI":"10.1093\/nar\/gkl092","volume":"34","author":"F Armougom","year":"2006","unstructured":"Armougom, F. et al. Expresso: automatic incorporation of structural information in multiple sequence alignments using 3D-Coffee. Nucleic Acids Res. 34, W604\u20138 (2006).","journal-title":"Nucleic Acids Res."},{"key":"51174_CR54","doi-asserted-by":"crossref","first-page":"W320","DOI":"10.1093\/nar\/gku316","volume":"42","author":"X Robert","year":"2014","unstructured":"Robert, X. & Gouet, P. Deciphering key features in protein structures with the new ENDscript server. Nucleic Acids Res. 42, W320\u20134 (2014).","journal-title":"Nucleic Acids Res."},{"key":"51174_CR55","doi-asserted-by":"crossref","first-page":"W529","DOI":"10.1093\/nar\/gkq399","volume":"38","author":"H Ashkenazy","year":"2010","unstructured":"Ashkenazy, H., Erez, E., Martz, E., Pupko, T. & Ben-Tal, N. ConSurf 2010: calculating evolutionary conservation in sequence and structure of proteins and nucleic acids. Nucleic Acids Res. 38, W529\u201333 (2010).","journal-title":"Nucleic Acids Res."}],"container-title":["Scientific Reports"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.nature.com\/articles\/s41598-019-51174-0.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/s41598-019-51174-0","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/s41598-019-51174-0.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,12,17]],"date-time":"2022-12-17T14:36:33Z","timestamp":1671287793000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.nature.com\/articles\/s41598-019-51174-0"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2019,10,10]]},"references-count":55,"journal-issue":{"issue":"1","published-online":{"date-parts":[[2019,12]]}},"alternative-id":["51174"],"URL":"https:\/\/doi.org\/10.1038\/s41598-019-51174-0","relation":{},"ISSN":["2045-2322"],"issn-type":[{"value":"2045-2322","type":"electronic"}],"subject":[],"published":{"date-parts":[[2019,10,10]]},"assertion":[{"value":"22 February 2019","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"25 September 2019","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"10 October 2019","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"The authors declare no competing interests.","order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Competing Interests"}}],"article-number":"14607"}}