An insight into the interaction mode between CheB and chemoreceptor from two crystal structures of CheB methylesterase catalytic domain
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Cho, Kwang-Hwi | - |
dc.contributor.author | Crane, Brian R. | - |
dc.contributor.author | Park, SangYoun | - |
dc.date.available | 2018-05-10T08:38:44Z | - |
dc.date.created | 2018-04-17 | - |
dc.date.issued | 2011-07-22 | - |
dc.identifier.issn | 0006-291X | - |
dc.identifier.uri | http://scholarworks.bwise.kr/ssu/handle/2018.sw.ssu/13619 | - |
dc.description.abstract | We have determined 2.2 angstrom resolution crystal structure of Thermotoga maritima CheB methylesterase domain to provide insight into the interaction mode between CheB and chemoreceptors. T. maritima CheB methylesterase domain has identical topology of a modified doubly-wound alpha/beta fold that was observed from the previously reported Salmonella typhimurium counterpart, but the analysis of the electrostatic potential surface near the catalytic triad indicated considerable charge distribution difference. As the CheB demethylation consensus sites of the chemoreceptors, the CheB substrate, are not uniquely conserved between T. maritima and S. typhimurium, such surfaces with differing electrostatic properties may reflect CheB regions that mediate protein-protein interaction. Via the computational docking of the two T. maritima and S. typhimurium CheB structures to the respective T. maritima and Escherichia colt chemoreceptors, we propose a CheB:chemoreceptor interaction mode. (C) 2011 Elsevier Inc. All rights reserved. | - |
dc.publisher | ACADEMIC PRESS INC ELSEVIER SCIENCE | - |
dc.relation.isPartOf | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | - |
dc.subject | CHEMOTAXIS RECEPTOR | - |
dc.subject | BACTERIAL CHEMOTAXIS | - |
dc.subject | REGULATORY DOMAIN | - |
dc.subject | METHYLTRANSFERASE CHER | - |
dc.subject | SIGNAL-TRANSDUCTION | - |
dc.subject | PHOSPHORYLATION | - |
dc.subject | REFINEMENT | - |
dc.subject | PROTEINS | - |
dc.subject | DYNAMICS | - |
dc.subject | SITES | - |
dc.title | An insight into the interaction mode between CheB and chemoreceptor from two crystal structures of CheB methylesterase catalytic domain | - |
dc.type | Article | - |
dc.identifier.doi | 10.1016/j.bbrc.2011.06.090 | - |
dc.type.rims | ART | - |
dc.identifier.bibliographicCitation | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.411, no.1, pp.69 - 75 | - |
dc.description.journalClass | 1 | - |
dc.identifier.wosid | 000293368000012 | - |
dc.identifier.scopusid | 2-s2.0-79960560342 | - |
dc.citation.endPage | 75 | - |
dc.citation.number | 1 | - |
dc.citation.startPage | 69 | - |
dc.citation.title | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | - |
dc.citation.volume | 411 | - |
dc.contributor.affiliatedAuthor | Cho, Kwang-Hwi | - |
dc.contributor.affiliatedAuthor | Park, SangYoun | - |
dc.type.docType | Article | - |
dc.description.oadoiVersion | accept | - |
dc.subject.keywordAuthor | CheB | - |
dc.subject.keywordAuthor | Methylesterase | - |
dc.subject.keywordAuthor | Thermotoga maritima | - |
dc.subject.keywordAuthor | Chemoreceptor | - |
dc.subject.keywordAuthor | Methyl-accepting chemotaxis proteins | - |
dc.subject.keywordAuthor | Protein-protein interaction | - |
dc.subject.keywordPlus | CHEMOTAXIS RECEPTOR | - |
dc.subject.keywordPlus | BACTERIAL CHEMOTAXIS | - |
dc.subject.keywordPlus | REGULATORY DOMAIN | - |
dc.subject.keywordPlus | METHYLTRANSFERASE CHER | - |
dc.subject.keywordPlus | SIGNAL-TRANSDUCTION | - |
dc.subject.keywordPlus | PHOSPHORYLATION | - |
dc.subject.keywordPlus | REFINEMENT | - |
dc.subject.keywordPlus | PROTEINS | - |
dc.subject.keywordPlus | DYNAMICS | - |
dc.subject.keywordPlus | SITES | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
Items in ScholarWorks are protected by copyright, with all rights reserved, unless otherwise indicated.
Soongsil University Library 369 Sangdo-Ro, Dongjak-Gu, Seoul, Korea (06978)02-820-0733
COPYRIGHT ⓒ SOONGSIL UNIVERSITY, ALL RIGHTS RESERVED.
Certain data included herein are derived from the © Web of Science of Clarivate Analytics. All rights reserved.
You may not copy or re-distribute this material in whole or in part without the prior written consent of Clarivate Analytics.