{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,4]],"date-time":"2026-10-04T21:08:21Z","timestamp":1791148101927,"version":"4.1.0"},"reference-count":42,"publisher":"Public Library of Science (PLoS)","issue":"5","license":[{"start":{"date-parts":[[2011,5,9]],"date-time":"2011-05-09T00:00:00Z","timestamp":1304899200000},"content-version":"unspecified","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["www.plosone.org"],"crossmark-restriction":false},"short-container-title":["PLoS ONE"],"DOI":"10.1371\/journal.pone.0019589","type":"journal-article","created":{"date-parts":[[2011,5,9]],"date-time":"2011-05-09T20:56:08Z","timestamp":1304974568000},"page":"e19589","update-policy":"https:\/\/doi.org\/10.1371\/journal.pone.corrections_policy","source":"Crossref","is-referenced-by-count":29,"title":["Crystal Structures of Two Aminoglycoside Kinases Bound with a Eukaryotic Protein Kinase Inhibitor"],"prefix":"10.1371","volume":"6","author":[{"given":"Desiree H.","family":"Fong","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bing","family":"Xiong","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jiyoung","family":"Hwang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Albert M.","family":"Berghuis","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"340","published-online":{"date-parts":[[2011,5,9]]},"reference":[{"key":"ref1","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1086\/595011","article-title":"Bad bugs, no drugs: no ESKAPE! An update from the Infectious Diseases Society of America.","volume":"48","author":"HW Boucher","year":"2009","journal-title":"Clinical infectious diseases: an official publication of the Infectious Diseases Society of America"},{"key":"ref2","doi-asserted-by":"crossref","first-page":"1325","DOI":"10.1002\/cbic.201000067","article-title":"Antibiotic resistance by enzyme inactivation: from mechanisms to solutions.","volume":"11","author":"G De Pascale","year":"2010","journal-title":"Chembiochem"},{"key":"ref3","doi-asserted-by":"crossref","first-page":"251","DOI":"10.1111\/j.1574-6976.2000.tb00541.x","article-title":"Molecular basis of antibiotic resistance and beta-lactamase inhibition by mechanism-based inactivators: perspectives and future directions.","volume":"24","author":"C Therrien","year":"2000","journal-title":"FEMS Microbiol Rev"},{"key":"ref4","doi-asserted-by":"crossref","first-page":"138","DOI":"10.1128\/MMBR.57.1.138-163.1993","article-title":"Molecular genetics of aminoglycoside resistance genes and familial relationships of the aminoglycoside-modifying enzymes.","volume":"57","author":"KJ Shaw","year":"1993","journal-title":"Microbiol Rev"},{"key":"ref5","doi-asserted-by":"crossref","first-page":"283","DOI":"10.1016\/S0163-7258(02)00197-3","article-title":"Protein kinase inhibitors and antibiotic resistance.","volume":"93","author":"DL Burk","year":"2002","journal-title":"Pharmacol Ther"},{"key":"ref6","doi-asserted-by":"crossref","first-page":"5273","DOI":"10.1021\/jm060732n","article-title":"Synthesis and structure-activity relationships of truncated bisubstrate inhibitors of aminoglycoside 6\u2032-N-acetyltransferases.","volume":"49","author":"F Gao","year":"2006","journal-title":"J Med Chem"},{"key":"ref7","doi-asserted-by":"crossref","first-page":"430","DOI":"10.1128\/CMR.16.3.430-450.2003","article-title":"Versatility of aminoglycosides and prospects for their future.","volume":"16","author":"SB Vakulenko","year":"2003","journal-title":"Clin Microbiol Rev"},{"key":"ref8","doi-asserted-by":"crossref","first-page":"887","DOI":"10.1016\/S0092-8674(00)80274-3","article-title":"Structure of an enzyme required for aminoglycoside antibiotic resistance reveals homology to eukaryotic protein kinases.","volume":"89","author":"WC Hon","year":"1997","journal-title":"Cell"},{"key":"ref9","doi-asserted-by":"crossref","first-page":"24755","DOI":"10.1074\/jbc.272.40.24755","article-title":"Inhibition of aminoglycoside antibiotic resistance enzymes by protein kinase inhibitors.","volume":"272","author":"DM Daigle","year":"1997","journal-title":"J Biol Chem"},{"key":"ref10","doi-asserted-by":"crossref","first-page":"2323","DOI":"10.1093\/emboj\/21.10.2323","article-title":"Substrate promiscuity of an aminoglycoside antibiotic resistance enzyme via target mimicry.","volume":"21","author":"DH Fong","year":"2002","journal-title":"Embo J"},{"key":"ref11","doi-asserted-by":"crossref","first-page":"9545","DOI":"10.1074\/jbc.M109.038364","article-title":"Structure of the Antibiotic Resistance Factor Spectinomycin Phosphotransferase from Legionella pneumophila.","volume":"285","author":"DH Fong","year":"2010","journal-title":"J Biol Chem"},{"key":"ref12","doi-asserted-by":"crossref","first-page":"491","DOI":"10.1016\/S0022-2836(03)00121-9","article-title":"The crystal structure of aminoglycoside-3\u2032-phosphotransferase-IIa, an enzyme responsible for antibiotic resistance.","volume":"327","author":"D Nurizzo","year":"2003","journal-title":"J Mol Biol"},{"key":"ref13","doi-asserted-by":"crossref","first-page":"4133","DOI":"10.1128\/JB.00149-09","article-title":"The crystal structures of substrate and nucleotide complexes of Enterococcus faecium aminoglycoside-2\u2033-phosphotransferase-IIa [APH(2\u2033)-IIa] provide insights into substrate selectivity in the APH(2\u2033) subfamily.","volume":"191","author":"PG Young","year":"2009","journal-title":"J Bacteriol"},{"key":"ref14","doi-asserted-by":"crossref","first-page":"1565","DOI":"10.1002\/pro.437","article-title":"Crystal structure and kinetic mechanism of aminoglycoside phosphotransferase-2\u2033-IVa.","volume":"19","author":"M Toth","year":"2010","journal-title":"Protein Sci"},{"key":"ref15","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1016\/S1074-5521(99)80016-7","article-title":"Aminoglycoside antibiotic phosphotransferases are also serine protein kinases.","volume":"6","author":"DM Daigle","year":"1999","journal-title":"Chem Biol"},{"key":"ref16","doi-asserted-by":"crossref","first-page":"6936","DOI":"10.1021\/bi00188a024","article-title":"Broad spectrum aminoglycoside phosphotransferase type III from Enterococcus: overexpression, purification, and substrate specificity.","volume":"33","author":"GA McKay","year":"1994","journal-title":"Biochemistry"},{"key":"ref17","doi-asserted-by":"crossref","first-page":"24686","DOI":"10.1074\/jbc.270.42.24686","article-title":"Kinetic mechanism of aminoglycoside phosphotransferase type IIIa. Evidence for a Theorell-Chance mechanism.","volume":"270","author":"GA McKay","year":"1995","journal-title":"J Biol Chem"},{"key":"ref18","doi-asserted-by":"crossref","first-page":"747","DOI":"10.1016\/S1074-5521(96)90251-3","article-title":"Mechanism of aminoglycoside 3\u2032-phosphotransferase type IIIa: His188 is not a phosphate-accepting residue.","volume":"3","author":"PR Thompson","year":"1996","journal-title":"Chem Biol"},{"key":"ref19","doi-asserted-by":"crossref","first-page":"30697","DOI":"10.1074\/jbc.274.43.30697","article-title":"The COOH terminus of aminoglycoside phosphotransferase (3\u2032)-IIIa is critical for antibiotic recognition and resistance.","volume":"274","author":"PR Thompson","year":"1999","journal-title":"J Biol Chem"},{"key":"ref20","doi-asserted-by":"crossref","first-page":"8756","DOI":"10.1021\/bi010504p","article-title":"Structural analyses of nucleotide binding to an aminoglycoside phosphotransferase.","volume":"40","author":"DL Burk","year":"2001","journal-title":"Biochemistry"},{"key":"ref21","doi-asserted-by":"crossref","first-page":"3049","DOI":"10.1128\/AAC.00062-09","article-title":"Structural basis of APH(3\u2032)-IIIa-mediated resistance to N1-substituted aminoglycoside antibiotics.","volume":"53","author":"DH Fong","year":"2009","journal-title":"Antimicrob Agents Chemother"},{"key":"ref22","doi-asserted-by":"crossref","first-page":"4924","DOI":"10.1016\/S0021-9258(18)83679-1","article-title":"A newly synthesized selective casein kinase I inhibitor, N-(2-aminoethyl)-5-chloroisoquinoline-8-sulfonamide, and affinity purification of casein kinase I from bovine testis.","volume":"264","author":"T Chijiwa","year":"1989","journal-title":"J Biol Chem"},{"key":"ref23","doi-asserted-by":"crossref","first-page":"663","DOI":"10.2174\/0929867043455792","article-title":"Recent kinase and kinase inhibitor X-ray structures: mechanisms of inhibition and selectivity insights.","volume":"11","author":"M Cherry","year":"2004","journal-title":"Curr Med Chem"},{"key":"ref24","doi-asserted-by":"crossref","first-page":"409","DOI":"10.1021\/jm0608107","article-title":"Molecular recognition of protein kinase binding pockets for design of potent and selective kinase inhibitors.","volume":"50","author":"JJ Liao","year":"2007","journal-title":"J Med Chem"},{"key":"ref25","doi-asserted-by":"crossref","first-page":"6308","DOI":"10.1073\/pnas.93.13.6308","article-title":"Structural basis for selectivity of the isoquinoline sulfonamide family of protein kinase inhibitors.","volume":"93","author":"RM Xu","year":"1996","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref26","doi-asserted-by":"crossref","first-page":"157","DOI":"10.1016\/S0163-7258(98)00054-0","article-title":"Conformational diversity of catalytic cores of protein kinases.","volume":"82","author":"JM Sowadski","year":"1999","journal-title":"Pharmacol Ther"},{"key":"ref27","doi-asserted-by":"crossref","first-page":"5036","DOI":"10.1021\/bi00316a032","article-title":"Isoquinolinesulfonamides, novel and potent inhibitors of cyclic nucleotide dependent protein kinase and protein kinase C.","volume":"23","author":"H Hidaka","year":"1984","journal-title":"Biochemistry"},{"key":"ref28","doi-asserted-by":"crossref","first-page":"60","DOI":"10.1038\/sj.embor.7400048","article-title":"D4476, a cell-permeant inhibitor of CK1, suppresses the site-specific phosphorylation and nuclear exclusion of FOXO1a.","volume":"5","author":"G Rena","year":"2004","journal-title":"EMBO Rep"},{"key":"ref29","doi-asserted-by":"crossref","first-page":"198","DOI":"10.1093\/bioinformatics\/btp650","article-title":"Kinase selectivity potential for inhibitors targeting the ATP binding site: a network analysis.","volume":"26","author":"D Huang","year":"2010","journal-title":"Bioinformatics"},{"key":"ref30","doi-asserted-by":"crossref","first-page":"291","DOI":"10.1016\/j.drudis.2008.12.002","article-title":"Kinase-targeted libraries: the design and synthesis of novel, potent, and selective kinase inhibitors.","volume":"14","author":"I Akritopoulou-Zanze","year":"2009","journal-title":"Drug Discov Today"},{"key":"ref31","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1017\/S0033583508004745","article-title":"Protein kinase inhibitors: contributions from structure to clinical compounds.","volume":"42","author":"LN Johnson","year":"2009","journal-title":"Q Rev Biophys"},{"key":"ref32","doi-asserted-by":"crossref","first-page":"1897","DOI":"10.1107\/S0907444904019390","article-title":"Crystallization and preliminary crystallographic analysis of 3\u2032-aminoglycoside kinase type IIIa complexed with a eukaryotic protein kinase inhibitor, CKI-7.","volume":"60","author":"DH Fong","year":"2004","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"key":"ref33","doi-asserted-by":"crossref","first-page":"606","DOI":"10.1107\/S1744309105016301","article-title":"Crystallization and preliminary crystallographic analysis of an aminoglycoside kinase from Legionella pneumophila.","volume":"61","author":"CT Lemke","year":"2005","journal-title":"Acta Crystallogr Sect F Struct Biol Cryst Commun"},{"key":"ref34","doi-asserted-by":"crossref","first-page":"307","DOI":"10.1016\/S0076-6879(97)76066-X","article-title":"Processing of X-ray diffraction data collected in oscillation mode.","volume":"276","author":"Z Otwinowski","year":"1997","journal-title":"Methods Enzymol"},{"key":"ref35","doi-asserted-by":"crossref","first-page":"905","DOI":"10.1107\/S0907444998003254","article-title":"Crystallography &amp; NMR system: A new software suite for macromolecular structure determination.","volume":"54","author":"AT Brunger","year":"1998","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"key":"ref36","doi-asserted-by":"crossref","first-page":"8127","DOI":"10.1021\/ja00467a001","article-title":"Conformational analysis. 130. MM2. A hydrocarbon force field utilizing V1 and V2 torsional terms.","volume":"99","author":"NL Allinger","year":"1977","journal-title":"Journal of American Chemical Society"},{"key":"ref37","article-title":"Molecular Mechanics.","author":"U Burkert","year":"1982"},{"key":"ref38","doi-asserted-by":"crossref","first-page":"110","DOI":"10.1107\/S0108767390010224","article-title":"Improved methods for building protein models in electron density maps and the location of errors in these models.","volume":"47","author":"TA Jones","year":"1991","journal-title":"Acta Crystallogr A"},{"key":"ref39","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1107\/S0907444909052925","article-title":"PHENIX: a comprehensive Python-based system for macromolecular structure solution.","volume":"66","author":"PD Adams","year":"2010","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"key":"ref40","doi-asserted-by":"crossref","first-page":"486","DOI":"10.1107\/S0907444910007493","article-title":"Features and development of Coot.","volume":"66","author":"P Emsley","year":"2010","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"key":"ref41","doi-asserted-by":"crossref","first-page":"458","DOI":"10.1107\/S0907444905001617","article-title":"Likelihood-enhanced fast translation functions.","volume":"61","author":"AJ McCoy","year":"2005","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"key":"ref42","first-page":"760","article-title":"The CCP4 Suite: Programs for Protein Crystallography.","volume":"D50","year":"1994","journal-title":"Acta Crystallogr"}],"container-title":["PLoS ONE"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/dx.plos.org\/10.1371\/journal.pone.0019589","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,11,23]],"date-time":"2021-11-23T00:20:14Z","timestamp":1637626814000},"score":1,"resource":{"primary":{"URL":"https:\/\/dx.plos.org\/10.1371\/journal.pone.0019589"}},"subtitle":[],"editor":[{"given":"Annalisa","family":"Pastore","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"editor"}]}],"short-title":[],"issued":{"date-parts":[[2011,5,9]]},"references-count":42,"journal-issue":{"issue":"5","published-online":{"date-parts":[[2011,5,9]]}},"URL":"https:\/\/doi.org\/10.1371\/journal.pone.0019589","relation":{},"ISSN":["1932-6203"],"issn-type":[{"value":"1932-6203","type":"electronic"}],"subject":[],"published":{"date-parts":[[2011,5,9]]}}}