Crystal structure of the response regulator spr1814 from Streptococcus pneumoniae reveals unique interdomain contacts among NarL family proteins
DC Field | Value | Language |
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dc.contributor.author | Park, Ae Kyung | - |
dc.contributor.author | Moon, Jin Ho | - |
dc.contributor.author | Oh, Jae Soon | - |
dc.contributor.author | Lee, Ki Seog | - |
dc.contributor.author | Chi, Young Min | - |
dc.date.accessioned | 2021-09-06T02:22:15Z | - |
dc.date.available | 2021-09-06T02:22:15Z | - |
dc.date.created | 2021-06-14 | - |
dc.date.issued | 2013-04-26 | - |
dc.identifier.issn | 0006-291X | - |
dc.identifier.uri | https://scholar.korea.ac.kr/handle/2021.sw.korea/103474 | - |
dc.description.abstract | Spr1814 belongs to the NarL/FixJ subfamily of signal transduction response regulators (RR), and has been predicted to regulate the neighboring ABC transporter, which translocates antibiotic molecules in Streptococcus pneumoniae. Here, we report the crystal structure of full-length unphosphorylated spr1814 at 1.7 angstrom resolution. The asymmetric unit contains two spr1814 molecules, which display very different conformations. Through comparisons with other RRs structures, we concluded that one molecule adopts a general inactive conformation, whereas the other molecule adopts an intermediate conformation. The superposition of each molecule showed that rotational change of the effector domain occurred in intermediate conformational state, implying that domain rearrangement could occur upon phosphorylation. (C) 2013 Elsevier Inc. All rights reserved. | - |
dc.language | English | - |
dc.language.iso | en | - |
dc.publisher | ACADEMIC PRESS INC ELSEVIER SCIENCE | - |
dc.subject | DOMAIN | - |
dc.subject | FIXJ | - |
dc.subject | PHOSPHORYLATION | - |
dc.subject | 2-COMPONENT | - |
dc.subject | ACTIVATION | - |
dc.subject | INSIGHTS | - |
dc.title | Crystal structure of the response regulator spr1814 from Streptococcus pneumoniae reveals unique interdomain contacts among NarL family proteins | - |
dc.type | Article | - |
dc.contributor.affiliatedAuthor | Chi, Young Min | - |
dc.identifier.doi | 10.1016/j.bbrc.2013.03.065 | - |
dc.identifier.scopusid | 2-s2.0-84876808041 | - |
dc.identifier.wosid | 000318751900011 | - |
dc.identifier.bibliographicCitation | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.434, no.1, pp.65 - 69 | - |
dc.relation.isPartOf | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | - |
dc.citation.title | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | - |
dc.citation.volume | 434 | - |
dc.citation.number | 1 | - |
dc.citation.startPage | 65 | - |
dc.citation.endPage | 69 | - |
dc.type.rims | ART | - |
dc.type.docType | Article | - |
dc.description.journalClass | 1 | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
dc.relation.journalResearchArea | Biophysics | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.relation.journalWebOfScienceCategory | Biophysics | - |
dc.subject.keywordPlus | DOMAIN | - |
dc.subject.keywordPlus | FIXJ | - |
dc.subject.keywordPlus | PHOSPHORYLATION | - |
dc.subject.keywordPlus | 2-COMPONENT | - |
dc.subject.keywordPlus | ACTIVATION | - |
dc.subject.keywordPlus | INSIGHTS | - |
dc.subject.keywordAuthor | Two-component phosphotransfer pathways | - |
dc.subject.keywordAuthor | Response regulators | - |
dc.subject.keywordAuthor | NarL subfamily | - |
dc.subject.keywordAuthor | Helix-turn-helix fold | - |
dc.subject.keywordAuthor | Streptococcus pneumoniae | - |
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