{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,13]],"date-time":"2026-04-13T06:46:26Z","timestamp":1776062786210,"version":"3.50.1"},"reference-count":58,"publisher":"Elsevier BV","issue":"20","license":[{"start":{"date-parts":[[2015,10,1]],"date-time":"2015-10-01T00:00:00Z","timestamp":1443657600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"funder":[{"DOI":"10.13039\/501100003074","name":"Agencia Nacional de Promoci\u00f3n Cient\u00edfica y Tecnol\u00f3gica","doi-asserted-by":"publisher","award":["PICT-2013-1629"],"award-info":[{"award-number":["PICT-2013-1629"]}],"id":[{"id":"10.13039\/501100003074","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Journal of Molecular Biology"],"published-print":{"date-parts":[[2015,10]]},"DOI":"10.1016\/j.jmb.2015.06.010","type":"journal-article","created":{"date-parts":[[2015,6,23]],"date-time":"2015-06-23T06:11:30Z","timestamp":1435039890000},"page":"3258-3272","source":"Crossref","is-referenced-by-count":21,"title":["Snapshots of Conformational Changes Shed Light into the NtrX Receiver Domain Signal Transduction Mechanism"],"prefix":"10.1016","volume":"427","author":[{"given":"Ignacio","family":"Fern\u00e1ndez","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Lisandro H.","family":"Otero","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Sebasti\u00e1n","family":"Klinke","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Mariela del Carmen","family":"Carrica","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Fernando A.","family":"Goldbaum","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.jmb.2015.06.010_bb0005","doi-asserted-by":"crossref","first-page":"183","DOI":"10.1146\/annurev.biochem.69.1.183","article-title":"Two-component signal transduction","volume":"69","author":"Stock","year":"2000","journal-title":"Annu Rev Biochem"},{"key":"10.1016\/j.jmb.2015.06.010_bb0010","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1146\/annurev.micro.091208.073214","article-title":"Biological insights from structures of two-component proteins","volume":"63","author":"Gao","year":"2009","journal-title":"Annu Rev Microbiol"},{"key":"10.1016\/j.jmb.2015.06.010_bb0015","doi-asserted-by":"crossref","first-page":"718","DOI":"10.1073\/pnas.89.2.718","article-title":"Phosphorylation of bacterial response regulator proteins by low molecular weight phospho-donors","volume":"89","author":"Lukat","year":"1992","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.1016\/j.jmb.2015.06.010_bb0020","doi-asserted-by":"crossref","first-page":"14965","DOI":"10.1021\/bi9715573","article-title":"Catalytic mechanism of phosphorylation and dephosphorylation of CheY: kinetic characterization of imidazole phosphates as phosphodonors and the role of acid catalysis","volume":"36","author":"Silversmith","year":"1997","journal-title":"Biochemistry"},{"key":"10.1016\/j.jmb.2015.06.010_bb0025","doi-asserted-by":"crossref","first-page":"323","DOI":"10.1016\/S0014-5793(99)01057-1","article-title":"Kinetics of CheY phosphorylation by small molecule phosphodonors","volume":"457","author":"Da Re","year":"1999","journal-title":"FEBS Lett"},{"key":"10.1016\/j.jmb.2015.06.010_bb0030","doi-asserted-by":"crossref","first-page":"14789","DOI":"10.1073\/pnas.96.26.14789","article-title":"Beryllofluoride mimics phosphorylation of NtrC and other bacterial response regulators","volume":"96","author":"Yan","year":"1999","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.1016\/j.jmb.2015.06.010_bb0035","doi-asserted-by":"crossref","first-page":"213","DOI":"10.3201\/eid0302.970219","article-title":"Brucellosis: an overview","volume":"3","author":"Corbel","year":"1997","journal-title":"Emerg Infect Dis"},{"key":"10.1016\/j.jmb.2015.06.010_bb0040","doi-asserted-by":"crossref","first-page":"15711","DOI":"10.1073\/pnas.232454299","article-title":"The analysis of the intramacrophagic virulome of Brucella suis deciphers the environment encountered by the pathogen inside the macrophage host cell","volume":"99","author":"Kohler","year":"2002","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.1016\/j.jmb.2015.06.010_bb0045","doi-asserted-by":"crossref","first-page":"1024","DOI":"10.1086\/319608","article-title":"Current understanding and management of chronic hepatosplenic suppurative brucellosis","volume":"32","author":"Ariza","year":"2001","journal-title":"Clin Infect Dis"},{"key":"10.1016\/j.jmb.2015.06.010_bb0050","doi-asserted-by":"crossref","first-page":"159","DOI":"10.1016\/S0732-8893(01)00344-3","article-title":"Chronic hepatosplenic abscesses in Brucellosis. Clinico-therapeutic features and molecular diagnostic approach","volume":"42","author":"Colmenero Jde","year":"2002","journal-title":"Diagn Microbiol Infect Dis"},{"key":"10.1016\/j.jmb.2015.06.010_bb0055","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1111\/j.1365-2958.2012.08095.x","article-title":"The NtrY\/X two-component system of Brucella spp. acts as a redox sensor and regulates the expression of nitrogen respiration enzymes","volume":"85","author":"Carrica Mdel","year":"2012","journal-title":"Mol Microbiol"},{"key":"10.1016\/j.jmb.2015.06.010_bb0060","doi-asserted-by":"crossref","first-page":"222","DOI":"10.1111\/mmi.12181","article-title":"The two-component systems PrrBA and NtrYX co-ordinately regulate the adaptation of Brucella abortus to an oxygen-limited environment","volume":"88","author":"Carrica Mdel","year":"2013","journal-title":"Mol Microbiol"},{"key":"10.1016\/j.jmb.2015.06.010_bb0065","doi-asserted-by":"crossref","first-page":"124","DOI":"10.1007\/BF00293830","article-title":"Characterization of a novel Azorhizobium caulinodans ORS571 two-component regulatory system, NtrY\/NtrX, involved in nitrogen fixation and metabolism","volume":"231","author":"Pawlowski","year":"1991","journal-title":"Mol Gen Genet"},{"key":"10.1016\/j.jmb.2015.06.010_bb0070","doi-asserted-by":"crossref","first-page":"5014","DOI":"10.1128\/IAI.00735-06","article-title":"Biochemical activities of three pairs of Ehrlichia chaffeensis two-component regulatory system proteins involved in inhibition of lysosomal fusion","volume":"74","author":"Kumagai","year":"2006","journal-title":"Infect Immun"},{"key":"10.1016\/j.jmb.2015.06.010_bb0075","doi-asserted-by":"crossref","first-page":"2632","DOI":"10.1128\/JB.02062-12","article-title":"Characterization of an ntrX mutant of Neisseria gonorrhoeae reveals a response regulator that controls expression of respiratory enzymes in oxidase-positive proteobacteria","volume":"195","author":"Atack","year":"2013","journal-title":"J Bacteriol"},{"key":"10.1016\/j.jmb.2015.06.010_bb0080","doi-asserted-by":"crossref","first-page":"7150","DOI":"10.1128\/AEM.02225-13","article-title":"The Sinorhizobium meliloti ntrX gene is involved in succinoglycan production, motility, and symbiotic nodulation on alfalfa","volume":"79","author":"Wang","year":"2013","journal-title":"Appl Environ Microbiol"},{"key":"10.1016\/j.jmb.2015.06.010_bb0085","doi-asserted-by":"crossref","first-page":"e334","DOI":"10.1371\/journal.pbio.0030334","article-title":"Two-component signal transduction pathways regulating growth and cell cycle progression in a bacterium: a system-level analysis","volume":"3","author":"Skerker","year":"2005","journal-title":"PLoS Biol"},{"key":"10.1016\/j.jmb.2015.06.010_bb0090","doi-asserted-by":"crossref","first-page":"497","DOI":"10.1128\/MMBR.00006-12","article-title":"The role of bacterial enhancer binding proteins as specialized activators of sigma54-dependent transcription","volume":"76","author":"Bush","year":"2012","journal-title":"Microbiol Mol Biol Rev"},{"key":"10.1016\/j.jmb.2015.06.010_bb0095","doi-asserted-by":"crossref","first-page":"1884","DOI":"10.1101\/gad.12.12.1884","article-title":"A bacterial ATP-dependent, enhancer binding protein that activates the housekeeping RNA polymerase","volume":"12","author":"Bowman","year":"1998","journal-title":"Genes Dev"},{"key":"10.1016\/j.jmb.2015.06.010_bb0100","doi-asserted-by":"crossref","first-page":"995","DOI":"10.1046\/j.1365-2958.1999.01660.x","article-title":"The synthesis of Rhodobacter capsulatus HupSL hydrogenase is regulated by the two-component HupT\/HupR system","volume":"34","author":"Dischert","year":"1999","journal-title":"Mol Microbiol"},{"key":"10.1016\/j.jmb.2015.06.010_bb0105","doi-asserted-by":"crossref","first-page":"e02141","DOI":"10.1128\/mBio.02141-14","article-title":"Ehrlichia chaffeensis proliferation begins with NtrY\/NtrX and PutA\/GlnA upregulation and CtrA degradation induced by proline and glutamine uptake","volume":"5","author":"Cheng","year":"2014","journal-title":"MBio"},{"key":"10.1016\/j.jmb.2015.06.010_bb0110","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1016\/j.jmb.2008.10.027","article-title":"The HupR receiver domain crystal structure in its nonphospho and inhibitory phospho states","volume":"385","author":"Davies","year":"2009","journal-title":"J Mol Biol"},{"key":"10.1016\/j.jmb.2015.06.010_bb0115","doi-asserted-by":"crossref","first-page":"1326","DOI":"10.1096\/fj.00-0516fje","article-title":"A dimeric two-component receiver domain inhibits the sigma54-dependent ATPase in DctD","volume":"15","author":"Meyer","year":"2001","journal-title":"FASEB J"},{"key":"10.1016\/j.jmb.2015.06.010_bb0120","doi-asserted-by":"crossref","first-page":"242","DOI":"10.1016\/j.jmb.2005.08.003","article-title":"Negative regulation of AAA+ATPase assembly by two component receiver domains: a transcription activation mechanism that is conserved in mesophilic and extremely hyperthermophilic bacteria","volume":"353","author":"Doucleff","year":"2005","journal-title":"J Mol Biol"},{"key":"10.1016\/j.jmb.2015.06.010_bb0125","doi-asserted-by":"crossref","first-page":"142","DOI":"10.1016\/j.mib.2010.01.015","article-title":"Receiver domain structure and function in response regulator proteins","volume":"13","author":"Bourret","year":"2010","journal-title":"Curr Opin Microbiol"},{"key":"10.1016\/j.jmb.2015.06.010_bb0130","doi-asserted-by":"crossref","first-page":"774","DOI":"10.1016\/j.jmb.2007.05.022","article-title":"Inference of macromolecular assemblies from crystalline state","volume":"372","author":"Krissinel","year":"2007","journal-title":"J Mol Biol"},{"key":"10.1016\/j.jmb.2015.06.010_bb0135","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1016\/j.jmb.2005.03.059","article-title":"Structural analysis and solution studies of the activated regulatory domain of the response regulator ArcA: a symmetric dimer mediated by the alpha4-beta5-alpha5 face","volume":"349","author":"Toro-Roman","year":"2005","journal-title":"J Mol Biol"},{"key":"10.1016\/j.jmb.2015.06.010_bb0140","doi-asserted-by":"crossref","first-page":"1353","DOI":"10.1016\/j.str.2005.06.006","article-title":"Mechanism of activation for transcription factor PhoB suggested by different modes of dimerization in the inactive and active states","volume":"13","author":"Bachhawat","year":"2005","journal-title":"Structure"},{"key":"10.1016\/j.jmb.2015.06.010_bb0145","doi-asserted-by":"crossref","first-page":"28637","DOI":"10.1074\/jbc.C100295200","article-title":"A distinct meta-active conformation in the 1.1-\u00c5 resolution structure of wild-type ApoCheY","volume":"276","author":"Simonovic","year":"2001","journal-title":"J Biol Chem"},{"key":"10.1016\/j.jmb.2015.06.010_bb0150","doi-asserted-by":"crossref","first-page":"e02105","DOI":"10.1128\/mBio.02105-14","article-title":"Allosteric activation of bacterial response regulators: the role of the cognate histidine kinase beyond phosphorylation","volume":"5","author":"Trajtenberg","year":"2014","journal-title":"MBio"},{"key":"10.1016\/j.jmb.2015.06.010_bb0155","doi-asserted-by":"crossref","first-page":"246","DOI":"10.1016\/j.mib.2010.01.006","article-title":"Summary of useful methods for two-component system research","volume":"13","author":"Scharf","year":"2010","journal-title":"Curr Opin Microbiol"},{"key":"10.1016\/j.jmb.2015.06.010_bb0160","doi-asserted-by":"crossref","first-page":"21755","DOI":"10.1074\/jbc.M113.471763","article-title":"A link between dimerization and autophosphorylation of the response regulator PhoB","volume":"288","author":"Creager-Allen","year":"2013","journal-title":"J Biol Chem"},{"key":"10.1016\/j.jmb.2015.06.010_bb0165","doi-asserted-by":"crossref","first-page":"2262","DOI":"10.1021\/bi301654m","article-title":"Nonconserved active site residues modulate CheY autophosphorylation kinetics and phosphodonor preference","volume":"52","author":"Thomas","year":"2013","journal-title":"Biochemistry"},{"key":"10.1016\/j.jmb.2015.06.010_bb0170","doi-asserted-by":"crossref","first-page":"453","DOI":"10.1111\/j.1365-2958.2008.06296.x","article-title":"Two variable active site residues modulate response regulator phosphoryl group stability","volume":"69","author":"Thomas","year":"2008","journal-title":"Mol Microbiol"},{"key":"10.1016\/j.jmb.2015.06.010_bb0175","doi-asserted-by":"crossref","first-page":"145","DOI":"10.1016\/0378-1119(93)90088-K","article-title":"Mutants of the two-component regulatory protein FixJ of Rhizobium meliloti that have increased activity at the nifA promoter","volume":"134","author":"Weinstein","year":"1993","journal-title":"Gene"},{"key":"10.1016\/j.jmb.2015.06.010_bb0180","doi-asserted-by":"crossref","first-page":"2429","DOI":"10.1126\/science.291.5512.2429","article-title":"Two-state allosteric behavior in a single-domain signaling protein","volume":"291","author":"Volkman","year":"2001","journal-title":"Science"},{"key":"10.1016\/j.jmb.2015.06.010_bb0185","doi-asserted-by":"crossref","first-page":"7354","DOI":"10.1128\/JB.00637-06","article-title":"Switched or not?: the structure of unphosphorylated CheY bound to the N terminus of FliM","volume":"188","author":"Dyer","year":"2006","journal-title":"J Bacteriol"},{"key":"10.1016\/j.jmb.2015.06.010_bb0190","doi-asserted-by":"crossref","first-page":"624","DOI":"10.1016\/j.jmb.2006.03.050","article-title":"Crystal structures of beryllium fluoride-free and beryllium fluoride-bound CheY in complex with the conserved C-terminal peptide of CheZ reveal dual binding modes specific to CheY conformation","volume":"359","author":"Guhaniyogi","year":"2006","journal-title":"J Mol Biol"},{"key":"10.1016\/j.jmb.2015.06.010_bb0195","doi-asserted-by":"crossref","first-page":"1363","DOI":"10.1016\/j.str.2012.05.008","article-title":"Segmental motions, not a two-state concerted switch, underlie allostery in CheY","volume":"20","author":"McDonald","year":"2012","journal-title":"Structure"},{"key":"10.1016\/j.jmb.2015.06.010_bb0200","doi-asserted-by":"crossref","first-page":"9081","DOI":"10.1021\/bi0273866","article-title":"High-resolution solution structure of the beryllofluoride-activated NtrC receiver domain","volume":"42","author":"Hastings","year":"2003","journal-title":"Biochemistry"},{"key":"10.1016\/j.jmb.2015.06.010_bb0205","doi-asserted-by":"crossref","first-page":"2062","DOI":"10.1529\/biophysj.106.081950","article-title":"Insights into correlated motions and long-range interactions in CheY derived from molecular dynamics simulations","volume":"92","author":"Knaggs","year":"2007","journal-title":"Biophys J"},{"key":"10.1016\/j.jmb.2015.06.010_bb0210","doi-asserted-by":"crossref","first-page":"1109","DOI":"10.1016\/j.cell.2009.11.022","article-title":"Transient non-native hydrogen bonds promote activation of a signaling protein","volume":"139","author":"Gardino","year":"2009","journal-title":"Cell"},{"key":"10.1016\/j.jmb.2015.06.010_bb0215","doi-asserted-by":"crossref","first-page":"1058","DOI":"10.1016\/j.jmb.2008.10.024","article-title":"Structure and regulatory mechanism of Aquifex aeolicus NtrC4: variability and evolution in bacterial transcriptional regulation","volume":"384","author":"Batchelor","year":"2008","journal-title":"J Mol Biol"},{"key":"10.1016\/j.jmb.2015.06.010_bb0220","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1107\/S0907444909047337","article-title":"Xds","volume":"66","author":"Kabsch","year":"2010","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"key":"10.1016\/j.jmb.2015.06.010_bb0225","doi-asserted-by":"crossref","first-page":"447","DOI":"10.1107\/S0907444907002661","article-title":"Automated search-model discovery and preparation for structure solution by molecular replacement","volume":"63","author":"Keegan","year":"2007","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"key":"10.1016\/j.jmb.2015.06.010_bb0230","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1107\/S0907444910045749","article-title":"Overview of the CCP4 suite and current developments","volume":"67","author":"Winn","year":"2011","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"key":"10.1016\/j.jmb.2015.06.010_bb0235","doi-asserted-by":"crossref","first-page":"1964","DOI":"10.1096\/fj.02-0395fje","article-title":"Two-component signaling in the AAA+ATPase DctD: binding Mg2+ and BeF3- selects between alternate dimeric states of the receiver domain","volume":"16","author":"Park","year":"2002","journal-title":"FASEB J"},{"key":"10.1016\/j.jmb.2015.06.010_bb0240","doi-asserted-by":"crossref","first-page":"303","DOI":"10.1107\/S0907444910051218","article-title":"Improvement of molecular-replacement models with Sculptor","volume":"67","author":"Bunkoczi","year":"2011","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"key":"10.1016\/j.jmb.2015.06.010_bb0245","doi-asserted-by":"crossref","first-page":"658","DOI":"10.1107\/S0021889807021206","article-title":"Phaser crystallographic software","volume":"40","author":"McCoy","year":"2007","journal-title":"J Appl Crystallogr"},{"key":"10.1016\/j.jmb.2015.06.010_bb0250","doi-asserted-by":"crossref","first-page":"1002","DOI":"10.1107\/S0907444906022116","article-title":"The Buccaneer software for automated model building. 1. Tracing protein chains","volume":"62","author":"Cowtan","year":"2006","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"key":"10.1016\/j.jmb.2015.06.010_bb0255","doi-asserted-by":"crossref","first-page":"486","DOI":"10.1107\/S0907444910007493","article-title":"Features and development of Coot","volume":"66","author":"Emsley","year":"2010","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"key":"10.1016\/j.jmb.2015.06.010_bb0260","series-title":"BUSTER version 2.10.1","author":"Bricogne","year":"2014"},{"key":"10.1016\/j.jmb.2015.06.010_bb0265","doi-asserted-by":"crossref","first-page":"12","DOI":"10.1107\/S0907444909042073","article-title":"MolProbity: all-atom structure validation for macromolecular crystallography","volume":"66","author":"Chen","year":"2010","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"key":"10.1016\/j.jmb.2015.06.010_bb0270","doi-asserted-by":"crossref","first-page":"2256","DOI":"10.1107\/S0907444904026460","article-title":"Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions","volume":"60","author":"Krissinel","year":"2004","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"key":"10.1016\/j.jmb.2015.06.010_bb0275","doi-asserted-by":"crossref","first-page":"2947","DOI":"10.1093\/bioinformatics\/btm404","article-title":"Clustal W and Clustal X version 2.0","volume":"23","author":"Larkin","year":"2007","journal-title":"Bioinformatics"},{"key":"10.1016\/j.jmb.2015.06.010_bb0280","doi-asserted-by":"crossref","first-page":"195","DOI":"10.1093\/bioinformatics\/bti770","article-title":"The SWISS-MODEL workspace: a Web-based environment for protein structure homology modelling","volume":"22","author":"Arnold","year":"2006","journal-title":"Bioinformatics"},{"key":"10.1016\/j.jmb.2015.06.010_bb0285","doi-asserted-by":"crossref","first-page":"W252","DOI":"10.1093\/nar\/gku340","article-title":"SWISS-MODEL: modelling protein tertiary and quaternary structure using evolutionary information","volume":"42","author":"Biasini","year":"2014","journal-title":"Nucleic Acids Res"},{"key":"10.1016\/j.jmb.2015.06.010_bb0290","doi-asserted-by":"crossref","first-page":"D387","DOI":"10.1093\/nar\/gkn750","article-title":"The SWISS-MODEL repository and associated resources","volume":"37","author":"Kiefer","year":"2009","journal-title":"Nucleic Acids Res"}],"container-title":["Journal of Molecular Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0022283615003502?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0022283615003502?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2018,9,21]],"date-time":"2018-09-21T15:20:43Z","timestamp":1537543243000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0022283615003502"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2015,10]]},"references-count":58,"journal-issue":{"issue":"20","published-print":{"date-parts":[[2015,10]]}},"alternative-id":["S0022283615003502"],"URL":"https:\/\/doi.org\/10.1016\/j.jmb.2015.06.010","relation":{},"ISSN":["0022-2836"],"issn-type":[{"value":"0022-2836","type":"print"}],"subject":[],"published":{"date-parts":[[2015,10]]}}}