{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,8]],"date-time":"2026-09-08T12:25:37Z","timestamp":1788870337561,"version":"build-2803163510"},"reference-count":34,"publisher":"Elsevier BV","issue":"2","license":[{"start":{"date-parts":[[2005,9,1]],"date-time":"2005-09-01T00:00:00Z","timestamp":1125532800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2005,9,1]],"date-time":"2005-09-01T00:00:00Z","timestamp":1125532800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2005,9,1]],"date-time":"2005-09-01T00:00:00Z","timestamp":1125532800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2005,9,1]],"date-time":"2005-09-01T00:00:00Z","timestamp":1125532800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2005,9,1]],"date-time":"2005-09-01T00:00:00Z","timestamp":1125532800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2005,9,1]],"date-time":"2005-09-01T00:00:00Z","timestamp":1125532800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2005,9,1]],"date-time":"2005-09-01T00:00:00Z","timestamp":1125532800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000015","name":"U.S. Department of Energy","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100000015","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000097","name":"National Center for Research Resources","doi-asserted-by":"publisher","award":["P41RR01209"],"award-info":[{"award-number":["P41RR01209"]}],"id":[{"id":"10.13039\/100000097","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Molecular Biology"],"published-print":{"date-parts":[[2005,9]]},"DOI":"10.1016\/j.jmb.2005.07.046","type":"journal-article","created":{"date-parts":[[2005,8,3]],"date-time":"2005-08-03T16:41:29Z","timestamp":1123087289000},"page":"478-486","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":9,"title":["Structure of the E.coli Aspartate Transcarbamoylase Trapped in the Middle of the Catalytic Cycle"],"prefix":"10.1016","volume":"352","author":[{"given":"Kimberly A.","family":"Stieglitz","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kelly J.","family":"Dusinberre","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"James P.","family":"Cardia","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hiro","family":"Tsuruta","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Evan R.","family":"Kantrowitz","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.jmb.2005.07.046_bib1","doi-asserted-by":"crossref","first-page":"1643","DOI":"10.1073\/pnas.82.6.1643","article-title":"Structure at 2.9-\u00c5 resolution of aspartate carbamoyltransferase complexed with the bisubstrate analogue N-(phosphonacetyl)-l-aspartate","volume":"82","author":"Krause","year":"1985","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"10.1016\/j.jmb.2005.07.046_bib2","doi-asserted-by":"crossref","first-page":"361","DOI":"10.1073\/pnas.82.2.361","article-title":"Regeneration of active enzyme by formation of hybrids from inactive derivatives: implications for active sites shared between polypeptide chains of aspartate transcarbamoylase","volume":"82","author":"Robey","year":"1985","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"10.1016\/j.jmb.2005.07.046_bib3","doi-asserted-by":"crossref","first-page":"316","DOI":"10.1016\/0003-9861(87)90498-X","article-title":"Kinetic mechanism of native Escherichia coli aspartate transcarbamylase","volume":"259","author":"Hsuanyu","year":"1987","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.jmb.2005.07.046_bib4","doi-asserted-by":"crossref","first-page":"8881","DOI":"10.1073\/pnas.0503742102","article-title":"Structural basis for ordered substrate binding and cooperativity in aspartate transcarbamoylase","volume":"102","author":"Wang","year":"2005","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"10.1016\/j.jmb.2005.07.046_bib5","doi-asserted-by":"crossref","first-page":"725","DOI":"10.1016\/0022-2836(88)90365-8","article-title":"Complex of N-phosphonacetyl-l-aspartate with aspartate carbamoyltransferase: X-ray refinement, analysis of conformational changes and catalytic and allosteric mechanisms","volume":"204","author":"Ke","year":"1988","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2005.07.046_bib6","doi-asserted-by":"crossref","first-page":"66","DOI":"10.1016\/0014-5793(90)80706-O","article-title":"Structural kinetics of the allosteric transition of aspartate transcarbamoylase produced by physiological substrates","volume":"263","author":"Tsuruta","year":"1990","journal-title":"FEBS Letters"},{"key":"10.1016\/j.jmb.2005.07.046_bib7","doi-asserted-by":"crossref","first-page":"49755","DOI":"10.1074\/jbc.M208919200","article-title":"The role of intersubunit interactions for the stabilization of the T State of Escherichia coli aspartate transcarbamoylase","volume":"277","author":"Chan","year":"2002","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2005.07.046_bib8","doi-asserted-by":"crossref","first-page":"3724","DOI":"10.1021\/bi00467a019","article-title":"Heterotropic effectors promote a global conformational change in aspartate transcarbamoylase","volume":"29","author":"Eisenstein","year":"1990","journal-title":"Biochemistry"},{"key":"10.1016\/j.jmb.2005.07.046_bib9","doi-asserted-by":"crossref","first-page":"189","DOI":"10.1016\/0022-2836(85)90190-1","article-title":"Quaternary structure changes in aspartate transcarbamylase studied by X-ray solution scattering; signal transmission following effector binding","volume":"185","author":"Herv\u00e9","year":"1985","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2005.07.046_bib10","doi-asserted-by":"crossref","first-page":"1093","DOI":"10.1099\/13500872-141-5-1093","article-title":"Ammonia-dependent synthesis and metabolic channelling of carbamoyl phosphate in the hyperthermophilic archaeon Pyrococcus furiosus","volume":"141","author":"Legrain","year":"1995","journal-title":"Microbiology"},{"key":"10.1016\/j.jmb.2005.07.046_bib11","doi-asserted-by":"crossref","first-page":"729","DOI":"10.1002\/(SICI)1097-0134(19991201)37:4<729::AID-PROT21>3.0.CO;2-F","article-title":"Insights into the mechanism of catalysis and heterotropic regulation of E.coli aspartate transcarbamoylase based upon a structure of enzyme complexed with the bisubstrate analog N-phosphonacetyl-l-aspartate at 2.1\u00c5","volume":"37","author":"Jin","year":"1999","journal-title":"Proteins: Struct. Funct. Genet."},{"key":"10.1016\/j.jmb.2005.07.046_bib12","doi-asserted-by":"crossref","first-page":"853","DOI":"10.1016\/j.jmb.2004.06.002","article-title":"Monitoring the transition from the T to the R state in E.coli aspartate transcarbamoylase by X-ray crystallography: crystal structures of the E50A mutant in four distinct allosteric states","volume":"341","author":"Stieglitz","year":"2004","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2005.07.046_bib13","doi-asserted-by":"crossref","first-page":"1884","DOI":"10.1002\/pro.5560070905","article-title":"Anatomy of protein pockets and cavities: measurement of binding site geometry and implications for ligand design","volume":"7","author":"Liang","year":"1998","journal-title":"Protein Sci"},{"key":"10.1016\/j.jmb.2005.07.046_bib14","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1002\/(SICI)1099-1352(199601)9:1<1::AID-JMR241>3.0.CO;2-6","article-title":"Automated docking of flexible ligands: applications of AutoDock","volume":"9","author":"Goodsell","year":"1996","journal-title":"J. Mol. Recognit."},{"key":"10.1016\/j.jmb.2005.07.046_bib15","doi-asserted-by":"crossref","first-page":"423","DOI":"10.1038\/87582","article-title":"Direct structural evidence for a concerted allosteric transition in Escherichia coli aspartate transcarbamoylase","volume":"8","author":"Macol","year":"2001","journal-title":"Nature Struct. Biol."},{"key":"10.1016\/j.jmb.2005.07.046_bib16","doi-asserted-by":"crossref","first-page":"4205","DOI":"10.1073\/pnas.85.12.4205","article-title":"Three-dimensional structure of carbamyl phosphate and succinate bound to aspartate carbamyltransferase","volume":"85","author":"Gouaux","year":"1988","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"10.1016\/j.jmb.2005.07.046_bib17","doi-asserted-by":"crossref","first-page":"6415","DOI":"10.1021\/bi030213b","article-title":"Aspartate transcarbamylase (ATCase) of Escherichia coli: a new crystalline R-state bound to PALA, or to product analogues citrate and phosphate","volume":"43","author":"Huang","year":"2004","journal-title":"Biochemistry"},{"key":"10.1016\/j.jmb.2005.07.046_bib18","doi-asserted-by":"crossref","first-page":"389","DOI":"10.1021\/bi00454a013","article-title":"Crystal structures of phosphonoacetamide ligated T and phosphonoacetamide and malonate ligated R states of aspartate carbamoyltransferase at 2.8\u00c5 resolution and neutral pH","volume":"29","author":"Gouaux","year":"1990","journal-title":"Biochemistry"},{"key":"10.1016\/j.jmb.2005.07.046_bib19","doi-asserted-by":"crossref","first-page":"2309","DOI":"10.1073\/pnas.87.6.2309","article-title":"The regulatory subunit of Escherichia coli aspartate carbamoyltransferase may influence homotropic cooperativity and heterotropic interactions by a direct interaction with the 240s loop of the catalytic chain","volume":"87","author":"Newton","year":"1990","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"10.1016\/j.jmb.2005.07.046_bib20","doi-asserted-by":"crossref","first-page":"12504","DOI":"10.1021\/bi00164a030","article-title":"The tryptophan residues of aspartate transcarbamylase: site-directed mutagenesis and time-resolved fluorescence spectroscopy","volume":"31","author":"Fetler","year":"1992","journal-title":"Biochemistry"},{"key":"10.1016\/j.jmb.2005.07.046_bib21","doi-asserted-by":"crossref","first-page":"945","DOI":"10.1074\/jbc.M304018200","article-title":"A fluorescent probe-labeled aspartate transcarbamoylase that monitors the allosteric conformational state","volume":"279","author":"West","year":"2004","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2005.07.046_bib22","doi-asserted-by":"crossref","first-page":"14712","DOI":"10.1016\/S0021-9258(17)38630-1","article-title":"Superproduction and rapid purification of E.coli aspartate transcarbamoylase and its catalytic subunit under extreme derepression of the pyrimidine pathway","volume":"260","author":"Nowlan","year":"1985","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2005.07.046_bib23","doi-asserted-by":"crossref","first-page":"10150","DOI":"10.1021\/bi00089a034","article-title":"The conserved residues glutamate-37, asparate-100 and arginine-269 are important for the structural stabilization of Escherichia coli aspartate transcarbamoylase","volume":"32","author":"Baker","year":"1993","journal-title":"Biochemistry"},{"key":"10.1016\/j.jmb.2005.07.046_bib24","doi-asserted-by":"crossref","first-page":"248","DOI":"10.1016\/0003-2697(76)90527-3","article-title":"A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding","volume":"72","author":"Bradford","year":"1976","journal-title":"Anal. Biochem."},{"key":"10.1016\/j.jmb.2005.07.046_bib25","doi-asserted-by":"crossref","first-page":"680","DOI":"10.1038\/227680a0","article-title":"Cleavage of structural proteins during the assembly of the head of bacteriophage T4","volume":"227","author":"Laemmli","year":"1970","journal-title":"Nature"},{"key":"10.1016\/j.jmb.2005.07.046_bib26","doi-asserted-by":"crossref","first-page":"680","DOI":"10.1111\/j.1749-6632.1964.tb14213.x","article-title":"Disc electrophoresis-II Method and application to human serum proteins","volume":"121","author":"Davis","year":"1964","journal-title":"Ann. N.Y. Acad. Sci."},{"key":"10.1016\/j.jmb.2005.07.046_bib27","doi-asserted-by":"crossref","first-page":"321","DOI":"10.1111\/j.1749-6632.1964.tb14207.x","article-title":"Disc electrophoresis. I. Background and theory","volume":"121","author":"Ornstein","year":"1964","journal-title":"Ann. N.Y. Acad. Sci."},{"key":"10.1016\/j.jmb.2005.07.046_bib28","doi-asserted-by":"crossref","first-page":"1718","DOI":"10.1107\/S090744499900935X","article-title":"The finer things in X-ray diffraction data collection","volume":"55","author":"Pflugrath","year":"1999","journal-title":"Acta Crystallog. sect. D"},{"key":"10.1016\/j.jmb.2005.07.046_bib29","doi-asserted-by":"crossref","first-page":"7702","DOI":"10.1021\/bi00485a020","article-title":"Crystal structures of aspartate carbamoyltransferase ligated with phosphonoacetamide, malonate and CTP or ATP at 2.8\u00c5 resolution and neutral pH","volume":"29","author":"Gouaux","year":"1990","journal-title":"Biochemistry"},{"key":"10.1016\/j.jmb.2005.07.046_bib30","doi-asserted-by":"crossref","first-page":"905","DOI":"10.1107\/S0907444998003254","article-title":"Crystallography and NMR system (CNS): a new software system for macromolecular structure determination","volume":"54","author":"Brunger","year":"1998","journal-title":"Acta Crystallog. sect. D"},{"key":"10.1016\/j.jmb.2005.07.046_bib31","doi-asserted-by":"crossref","first-page":"156","DOI":"10.1006\/jsbi.1999.4094","article-title":"XtalView\/Xfit\u2013A versatile program for manipulating atomic coordinates and electron density","volume":"125","author":"McRee","year":"1999","journal-title":"J. Struct. Biol."},{"key":"10.1016\/j.jmb.2005.07.046_bib32","doi-asserted-by":"crossref","first-page":"283","DOI":"10.1107\/S0021889892009944","article-title":"PROCHECK: a program to check the stereochemical quality of protein structures","volume":"26","author":"Laskowski","year":"1993","journal-title":"J. Appl. Crystallog."},{"key":"10.1016\/j.jmb.2005.07.046_bib33","doi-asserted-by":"crossref","first-page":"944","DOI":"10.1107\/S0021889803006721","article-title":"POVScript+: a program for model and data visualization using persistence of vision ray-tracing","volume":"36","author":"Fenn","year":"2003","journal-title":"J. Appl. Crystallog."},{"key":"10.1016\/j.jmb.2005.07.046_bib34","doi-asserted-by":"crossref","first-page":"1605","DOI":"10.1002\/jcc.20084","article-title":"UCSF Chimera - a visualization system for exploratory research and analysis","volume":"25","author":"Pettersen","year":"2004","journal-title":"J. Comput. Chem."}],"container-title":["Journal of Molecular Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0022283605008478?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0022283605008478?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,11,9]],"date-time":"2025-11-09T06:04:42Z","timestamp":1762668282000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0022283605008478"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2005,9]]},"references-count":34,"journal-issue":{"issue":"2","published-print":{"date-parts":[[2005,9]]}},"alternative-id":["S0022283605008478"],"URL":"https:\/\/doi.org\/10.1016\/j.jmb.2005.07.046","relation":{},"ISSN":["0022-2836"],"issn-type":[{"value":"0022-2836","type":"print"}],"subject":[],"published":{"date-parts":[[2005,9]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Structure of the E.coli Aspartate Transcarbamoylase Trapped in the Middle of the Catalytic Cycle","name":"articletitle","label":"Article Title"},{"value":"Journal of Molecular Biology","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.jmb.2005.07.046","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"Copyright \u00a9 2005 Published by Elsevier Ltd.","name":"copyright","label":"Copyright"}]}}