DC Field | Value | Language |
---|---|---|
dc.contributor.author | Jo, H | - |
dc.contributor.author | Jeong, EY | - |
dc.contributor.author | Jeon, J | - |
dc.contributor.author | Ban, C | - |
dc.date.accessioned | 2015-06-25T01:35:10Z | - |
dc.date.available | 2015-06-25T01:35:10Z | - |
dc.date.created | 2015-02-04 | - |
dc.date.issued | 2014-12-05 | - |
dc.identifier.issn | 1472-6807 | - |
dc.identifier.other | 2015-OAK-0000031442 | en_US |
dc.identifier.uri | https://oasis.postech.ac.kr/handle/2014.oak/9861 | - |
dc.description.abstract | Background: Polymyxin B resistance protein D (PmrD) plays a key role in the polymyxin B-resistance pathway, as it is the signaling protein that can act as a specific connecter between PmrA/PmrB and PhoP/PhoQ. We conducted structural analysis to characterize Escherichia coli (E. coli) PmrD, which exhibits different features compared with PmrD in other bacteria. Results: The X-ray crystal structure of E. coli PmrD was determined at a 2.00 angstrom resolution, revealing novel information such as the unambiguous secondary structures of the protein and the presence of a disulfide bond. Furthermore, various assays such as native gel electrophoresis, surface plasmon resonance (SPR), size-exclusion chromatography, dynamic light scattering (DLS), and small-angle X-ray scattering (SAXS) measurements, were performed to elucidate the structural and functional role of the internal disulfide bond in E. coli PmrD. Conclusions: The structural characteristics of E. coli PmrD were clearly identified via diverse techniques. The findings help explain the different protective mechanism of E. coli compared to other Gram-negative bacteria. | - |
dc.description.statementofresponsibility | open | en_US |
dc.language | English | - |
dc.publisher | BIOMED CENTRAL LTD | - |
dc.relation.isPartOf | BMC STRUCTURAL BIOLOGY | - |
dc.rights | BY_NC_ND | en_US |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/2.0/kr | en_US |
dc.title | Structural insights into Escherichia coli polymyxin B resistance protein D with X-ray crystallography and small-angle X-ray scattering | - |
dc.type | Article | - |
dc.contributor.college | 화학과 | en_US |
dc.identifier.doi | 10.1186/S12900-014-0024-Y | - |
dc.author.google | Jo, H | en_US |
dc.author.google | Jeong, EY | en_US |
dc.author.google | Ban, C | en_US |
dc.author.google | Jeon, J | en_US |
dc.relation.volume | 14 | en_US |
dc.contributor.id | 10085220 | en_US |
dc.relation.journal | BMC STRUCTURAL BIOLOGY | en_US |
dc.relation.index | SCI급, SCOPUS 등재논문 | en_US |
dc.relation.sci | SCIE | en_US |
dc.collections.name | Journal Papers | en_US |
dc.type.rims | ART | - |
dc.identifier.bibliographicCitation | BMC STRUCTURAL BIOLOGY, v.14 | - |
dc.identifier.wosid | 000346089500001 | - |
dc.date.tcdate | 2019-01-01 | - |
dc.citation.title | BMC STRUCTURAL BIOLOGY | - |
dc.citation.volume | 14 | - |
dc.contributor.affiliatedAuthor | Ban, C | - |
dc.identifier.scopusid | 2-s2.0-84946826022 | - |
dc.description.journalClass | 1 | - |
dc.description.journalClass | 1 | - |
dc.description.wostc | 2 | - |
dc.description.scptc | 2 | * |
dc.date.scptcdate | 2018-10-274 | * |
dc.type.docType | Article | - |
dc.subject.keywordPlus | 2-COMPONENT REGULATORY SYSTEMS | - |
dc.subject.keywordPlus | SALMONELLA-TYPHIMURIUM | - |
dc.subject.keywordPlus | PROGRAM | - |
dc.subject.keywordPlus | PMRD | - |
dc.subject.keywordAuthor | PmrD | - |
dc.subject.keywordAuthor | E. coli | - |
dc.subject.keywordAuthor | SAXS | - |
dc.subject.keywordAuthor | Crystal structure | - |
dc.subject.keywordAuthor | Solution structure | - |
dc.subject.keywordAuthor | Mutational study | - |
dc.relation.journalWebOfScienceCategory | Biophysics | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Biophysics | - |
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