{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,5]],"date-time":"2026-05-05T20:27:48Z","timestamp":1778012868941,"version":"3.51.4"},"reference-count":28,"publisher":"Springer Science and Business Media LLC","issue":"6861","license":[{"start":{"date-parts":[[2001,11,1]],"date-time":"2001-11-01T00:00:00Z","timestamp":1004572800000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/www.springer.com\/tdm"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Nature"],"published-print":{"date-parts":[[2001,11]]},"DOI":"10.1038\/35104586","type":"journal-article","created":{"date-parts":[[2002,7,26]],"date-time":"2002-07-26T04:34:56Z","timestamp":1027658096000},"page":"325-329","source":"Crossref","is-referenced-by-count":216,"title":["Mechanism of ubiquitin activation revealed by the structure of a bacterial MoeB\u2013MoaD complex"],"prefix":"10.1038","volume":"414","author":[{"given":"Michael W.","family":"Lake","sequence":"first","affiliation":[]},{"given":"Margot M.","family":"Wuebbens","sequence":"additional","affiliation":[]},{"given":"K. V.","family":"Rajagopalan","sequence":"additional","affiliation":[]},{"given":"Hermann","family":"Schindelin","sequence":"additional","affiliation":[]}],"member":"297","reference":[{"key":"BF35104586_CR1","doi-asserted-by":"publisher","first-page":"563","DOI":"10.1126\/science.289.5479.563","volume":"289","author":"M Hochstrasser","year":"2000","unstructured":"Hochstrasser, M. All in the ubiquitin family. Science 289, 563\u2013564 (2000).","journal-title":"Science"},{"key":"BF35104586_CR2","doi-asserted-by":"publisher","first-page":"E153","DOI":"10.1038\/35019643","volume":"2","author":"M Hochstrasser","year":"2000","unstructured":"Hochstrasser, M. Evolution and function of ubiquitin-like protein-conjugation systems. Nature Cell Biol. 2, E153\u2013E157 (2000).","journal-title":"Nature Cell Biol."},{"key":"BF35104586_CR3","first-page":"674","volume-title":"Escherichia coli and Salmonella typhimurium: Cellular and Molecular Biology","author":"KV Rajagopalan","year":"1996","unstructured":"Rajagopalan, K. V. in Escherichia coli and Salmonella typhimurium: Cellular and Molecular Biology (ed. Neidhardt, F. C.) 674\u2013679 (ASM Press, Washington DC, 1996)."},{"key":"BF35104586_CR4","doi-asserted-by":"publisher","first-page":"757","DOI":"10.1042\/bst0250757","volume":"25","author":"KV Rajagopalan","year":"1997","unstructured":"Rajagopalan, K. V. Biosynthesis and processing of the molybdenum cofactors. Biochem. Soc. Trans. 25, 757\u2013761 (1997).","journal-title":"Biochem. Soc. Trans."},{"key":"BF35104586_CR5","doi-asserted-by":"publisher","first-page":"42","DOI":"10.1038\/87531","volume":"8","author":"MJ Rudolph","year":"2001","unstructured":"Rudolph, M. J., Wuebbens, M. M., Rajagopalan, K. V. & Schindelin, H. Crystal structure of molybdopterin synthase and its evolutionary relationship to ubiquitin activation. Nature Struct. Biol. 8, 42\u201346 (2001).","journal-title":"Nature Struct. Biol."},{"key":"BF35104586_CR6","doi-asserted-by":"publisher","first-page":"34695","DOI":"10.1074\/jbc.M102787200","volume":"276","author":"S Leimk\u00fchler","year":"2001","unstructured":"Leimk\u00fchler, S., Wuebbens, M. M. & Rajagopalan, K. V. Characterization of Escherichia coli MoeB and its involvement in the activation of MPT synthase for the biosynthesis of the molybdenum cofactor. J. Biol. Chem. 276, 34695\u201334701 (2001).","journal-title":"J. Biol. Chem."},{"key":"BF35104586_CR7","doi-asserted-by":"crossref","first-page":"13506","DOI":"10.1016\/S0021-9258(19)38678-8","volume":"268","author":"DM Pitterle","year":"1993","unstructured":"Pitterle, D. M., Johnson, J. L. & Rajagopalan, K. V. In vitro synthesis of molybdopterin from precursor Z using purified converting factor. J. Biol. Chem. 268, 13506\u201313509 (1993).","journal-title":"J. Biol. Chem."},{"key":"BF35104586_CR8","doi-asserted-by":"publisher","first-page":"945","DOI":"10.1002\/j.1460-2075.1982.tb01276.x","volume":"1","author":"JE Walker","year":"1982","unstructured":"Walker, J. E., Saraste, M., Runswick, M. J. & Gay, N. J. Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J. 1, 945\u2013951 (1982).","journal-title":"EMBO J."},{"key":"BF35104586_CR9","doi-asserted-by":"publisher","first-page":"7300","DOI":"10.1021\/bi00189a035","volume":"33","author":"TJ Burch","year":"1994","unstructured":"Burch, T. J. & Haas, A. L. Site-directed mutagenesis of ubiquitin. Differential roles for arginine in the interaction with ubiquitin-activating enzyme. Biochemistry 33, 7300\u20137308 (1994).","journal-title":"Biochemistry"},{"key":"BF35104586_CR10","doi-asserted-by":"publisher","first-page":"1449","DOI":"10.1006\/jmbi.1999.2562","volume":"286","author":"JG Arnez","year":"1999","unstructured":"Arnez, J. G., Dock-Bregeon, A. C. & Moras, D. Glycyl-tRNA synthetase uses a negatively charged pit for specific recognition and activation of glycine. J. Mol. Biol. 286, 1449\u20131459 (1999).","journal-title":"J. Mol. Biol."},{"key":"BF35104586_CR11","doi-asserted-by":"crossref","first-page":"14799","DOI":"10.1016\/S0021-9258(18)42110-2","volume":"267","author":"PM Hatfield","year":"1992","unstructured":"Hatfield, P. M. & Vierstra, R. D. Multiple forms of ubiquitin-activating enzyme E1 from wheat. J. Biol. Chem. 267, 14799\u201314803 (1992).","journal-title":"J. Biol. Chem."},{"key":"BF35104586_CR12","doi-asserted-by":"publisher","first-page":"20096","DOI":"10.1074\/jbc.M002680200","volume":"275","author":"CT Lauhon","year":"2000","unstructured":"Lauhon, C. T. & Kambampati, R. The iscS gene in Escherichia coli is required for the biosynthesis of 4-thiouridine, thiamin, and NAD. J. Biol. Chem. 275, 20096\u201320103 (2000).","journal-title":"J. Biol. Chem."},{"key":"BF35104586_CR13","doi-asserted-by":"publisher","first-page":"8283","DOI":"10.1074\/jbc.275.12.8283","volume":"275","author":"PM Palenchar","year":"2000","unstructured":"Palenchar, P. M., Buck, C. J., Cheng, H., Larson, T. J. & Mueller, E. G. Evidence that ThiI, an enzyme shared between thiamin and 4-thiouridine biosynthesis, may be a sulfurtransferase that proceeds through a persulfide intermediate. J. Biol. Chem. 275, 8283\u20138286 (2000).","journal-title":"J. Biol. Chem."},{"key":"BF35104586_CR14","doi-asserted-by":"publisher","first-page":"8513","DOI":"10.1073\/pnas.141226698","volume":"98","author":"J Xi","year":"2001","unstructured":"Xi, J., Ge, Y., Kinsland, C., McLafferty, F. W. & Begley, T. P. Biosynthesis of the thiazole moiety of thiamin in Escherichia coli: identification of an acyldisulfide-linked protein-protein conjugate that is functionally analogous to the ubiquitin\/E1 complex. Proc. Natl Acad. Sci. USA 98, 8513\u20138518 (2001).","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"BF35104586_CR15","doi-asserted-by":"publisher","first-page":"22024","DOI":"10.1074\/jbc.M102072200","volume":"276","author":"S Leimk\u00fchler","year":"2001","unstructured":"Leimk\u00fchler, S. & Rajagopalan, K. V. An Escherichia coli NifS-like sulfurtransferase is required for the transfer of cysteine sulfur in the in vitro synthesis of molybdopterin from precursor Z. J. Biol. Chem. 276, 22024\u201322031 (2001).","journal-title":"J. Biol. Chem."},{"key":"BF35104586_CR16","doi-asserted-by":"publisher","first-page":"307","DOI":"10.1016\/S0076-6879(97)76066-X","volume-title":"Methods in Enzymology: Macromolecular Crystallography","author":"Z Otwinowski","year":"1997","unstructured":"Otwinowski, Z. & Minor, W. in Methods in Enzymology: Macromolecular Crystallography (eds Carter, C. W. & Sweet, R. M. ) 307\u2013326 (Academic, San Diego, 1997)."},{"key":"BF35104586_CR17","doi-asserted-by":"publisher","first-page":"319","DOI":"10.1016\/S0076-6879(97)77018-6","volume-title":"Methods in Enzymology: Macromolecular Crystallography","author":"GM Sheldrick","year":"1997","unstructured":"Sheldrick, G. M. & Schneider, T. R. in Methods in Enzymology: Macromolecular Crystallography (eds Carter, C. W. & Sweet, R. M.) 319\u2013343 (Academic, San Diego, 1997)."},{"key":"BF35104586_CR18","doi-asserted-by":"publisher","first-page":"472","DOI":"10.1016\/S0076-6879(97)76073-7","volume-title":"Methods in Enzymology: Macromolecular Crystallography","author":"E DeLaFortelle","year":"1997","unstructured":"DeLaFortelle, E. & Bricogne, G. in Methods in Enzymology: Macromolecular Crystallography (eds Carter, C. W. & Sweet, R. M.) 472\u2013494 (Academic, San Diego, 1997)."},{"key":"BF35104586_CR19","doi-asserted-by":"publisher","first-page":"30","DOI":"10.1107\/S0907444995008754","volume":"52","author":"JP Abrahams","year":"1996","unstructured":"Abrahams, J. P. & Leslie, A. G. W. Methods used in the structure determination of bovine mitochondrial F1 ATPase. Acta Crystallogr. D 52, 30\u201342 (1996).","journal-title":"Acta Crystallogr. D"},{"key":"BF35104586_CR20","doi-asserted-by":"publisher","first-page":"458","DOI":"10.1038\/8263","volume":"6","author":"A Perrakis","year":"1999","unstructured":"Perrakis, A., Morris, R. & Lamzin, V. S. Automated protein model building combined with iterative structure refinement. Nature Struct. Biol. 6, 458\u2013463 (1999).","journal-title":"Nature Struct. Biol."},{"key":"BF35104586_CR21","doi-asserted-by":"publisher","first-page":"760","DOI":"10.1107\/S0907444993011898","volume":"50","author":"S Bailey","year":"1994","unstructured":"Bailey, S. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D 50, 760\u2013763 (1994).","journal-title":"Acta Crystallogr. D"},{"key":"BF35104586_CR22","doi-asserted-by":"publisher","first-page":"240","DOI":"10.1107\/S0907444996012255","volume":"53","author":"G Murshudov","year":"1997","unstructured":"Murshudov, G., Vagin, A. & Dodson, E. Refinement of macromolecular structures by the maximum likelihood method. Acta Crystallogr. D 53, 240\u2013255 (1997).","journal-title":"Acta Crystallogr. D"},{"key":"BF35104586_CR23","doi-asserted-by":"publisher","first-page":"110","DOI":"10.1107\/S0108767390010224","volume":"47","author":"TA Jones","year":"1991","unstructured":"Jones, T. A., Zou, J. Y., Cowan, S. W. & Kjeldgaard, M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47, 110\u2013119 (1991).","journal-title":"Acta Crystallogr. A"},{"key":"BF35104586_CR24","doi-asserted-by":"publisher","first-page":"110","DOI":"10.1128\/jb.169.1.110-116.1987","volume":"169","author":"ME Johnson","year":"1987","unstructured":"Johnson, M. E. & Rajagopalan, K. V. In vitro system for molybdopterin biosynthesis. J. Bacteriol. 169, 110\u2013116 (1987).","journal-title":"J. Bacteriol."},{"key":"BF35104586_CR25","doi-asserted-by":"publisher","first-page":"1049","DOI":"10.1006\/jmbi.1993.1351","volume":"231","author":"RA Laskowski","year":"1993","unstructured":"Laskowski, R. A., Moss, D. S. & Thornton, J. M. Main-chain bond lengths and bond angles in protein structures. J. Mol. Biol. 231, 1049\u20131067 (1993).","journal-title":"J. Mol. Biol."},{"key":"BF35104586_CR26","doi-asserted-by":"publisher","first-page":"946","DOI":"10.1107\/S0021889891004399","volume":"24","author":"PJ Kraulis","year":"1991","unstructured":"Kraulis, P. J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946\u2013950 (1991).","journal-title":"J. Appl. Crystallogr."},{"key":"BF35104586_CR27","doi-asserted-by":"publisher","first-page":"37","DOI":"10.1093\/protein\/6.1.37","volume":"6","author":"GJ Barton","year":"1993","unstructured":"Barton, G. J. ALSCRIPT: a tool to format multiple sequence alignments. Protein Eng. 6, 37\u201340 (1993).","journal-title":"Protein Eng."},{"key":"BF35104586_CR28","doi-asserted-by":"publisher","first-page":"281","DOI":"10.1002\/prot.340110407","volume":"11","author":"A Nicholls","year":"1991","unstructured":"Nicholls, A., Sharp, K. A. & Honig, B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11, 281\u2013296 (1991).","journal-title":"Proteins"}],"container-title":["Nature"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/www.nature.com\/articles\/35104586.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/www.nature.com\/articles\/35104586","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/www.nature.com\/doifinder\/10.1038\/35104586","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"},{"URL":"http:\/\/www.nature.com\/articles\/35104586.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,5,16]],"date-time":"2023-05-16T22:15:38Z","timestamp":1684275338000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.nature.com\/articles\/35104586"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2001,11]]},"references-count":28,"journal-issue":{"issue":"6861","published-print":{"date-parts":[[2001,11]]}},"alternative-id":["BF35104586"],"URL":"https:\/\/doi.org\/10.1038\/35104586","relation":{"has-review":[{"id-type":"doi","id":"10.3410\/f.1002471.26355","asserted-by":"object"},{"id-type":"doi","id":"10.3410\/f.1002471.31604","asserted-by":"object"},{"id-type":"doi","id":"10.3410\/f.1002471.29459","asserted-by":"object"}]},"ISSN":["0028-0836","1476-4687"],"issn-type":[{"value":"0028-0836","type":"print"},{"value":"1476-4687","type":"electronic"}],"subject":[],"published":{"date-parts":[[2001,11]]}}}