Structural characterization of the full-length response regulator spr1814 in complex with a phosphate analogue reveals a novel conformational plasticity of the linker region
DC Field | Value | Language |
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dc.contributor.author | Park, Ae Kyung | - |
dc.contributor.author | Lee, Jeong Hye | - |
dc.contributor.author | Chi, Young Min | - |
dc.contributor.author | Park, Hyun | - |
dc.date.accessioned | 2021-09-04T00:23:57Z | - |
dc.date.available | 2021-09-04T00:23:57Z | - |
dc.date.created | 2021-06-18 | - |
dc.date.issued | 2016-04-29 | - |
dc.identifier.issn | 0006-291X | - |
dc.identifier.uri | https://scholar.korea.ac.kr/handle/2021.sw.korea/88884 | - |
dc.description.abstract | Spr1814 of Streptococcus pneumoniae is a response regulator (RR) that belongs to the NarL/FixJ subfamily and has a four-helix helix-turn-helix DNA-binding domain. Here, the X-ray crystal structure of the full-length spr1814 in complex with a phosphate analogue beryllium fluoride (BeF3-) was determined at 2.0 angstrom. This allows for a structural comparison with the previously reported full-length unphosphorylated spr1814. The phosphorylation of conserved aspartic acid residue of N-terminal receiver domain triggers a structural perturbation at the alpha 4-beta 5-alpha 5 interface, leading to the domain reorganization of spr1814, and this is achieved by a rotational change in the C-terminal DNA-binding domain. (C) 2016 Elsevier Inc. All rights reserved. | - |
dc.language | English | - |
dc.language.iso | en | - |
dc.publisher | ACADEMIC PRESS INC ELSEVIER SCIENCE | - |
dc.subject | STREPTOCOCCUS-PNEUMONIAE | - |
dc.subject | CRYSTAL-STRUCTURES | - |
dc.subject | ESCHERICHIA-COLI | - |
dc.subject | RECEIVER DOMAIN | - |
dc.subject | DIMERIZATION | - |
dc.subject | 2-COMPONENT | - |
dc.subject | RECOGNITION | - |
dc.subject | ACTIVATION | - |
dc.subject | MECHANISM | - |
dc.subject | ABSENCE | - |
dc.title | Structural characterization of the full-length response regulator spr1814 in complex with a phosphate analogue reveals a novel conformational plasticity of the linker region | - |
dc.type | Article | - |
dc.contributor.affiliatedAuthor | Chi, Young Min | - |
dc.identifier.doi | 10.1016/j.bbrc.2016.03.144 | - |
dc.identifier.scopusid | 2-s2.0-84961967636 | - |
dc.identifier.wosid | 000374809700040 | - |
dc.identifier.bibliographicCitation | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.473, no.2, pp.625 - 629 | - |
dc.relation.isPartOf | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | - |
dc.citation.title | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | - |
dc.citation.volume | 473 | - |
dc.citation.number | 2 | - |
dc.citation.startPage | 625 | - |
dc.citation.endPage | 629 | - |
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 | STREPTOCOCCUS-PNEUMONIAE | - |
dc.subject.keywordPlus | CRYSTAL-STRUCTURES | - |
dc.subject.keywordPlus | ESCHERICHIA-COLI | - |
dc.subject.keywordPlus | RECEIVER DOMAIN | - |
dc.subject.keywordPlus | DIMERIZATION | - |
dc.subject.keywordPlus | 2-COMPONENT | - |
dc.subject.keywordPlus | RECOGNITION | - |
dc.subject.keywordPlus | ACTIVATION | - |
dc.subject.keywordPlus | MECHANISM | - |
dc.subject.keywordPlus | ABSENCE | - |
dc.subject.keywordAuthor | Two-component system | - |
dc.subject.keywordAuthor | Response regulator | - |
dc.subject.keywordAuthor | NarL subfamily | - |
dc.subject.keywordAuthor | Phosphorylation | - |
dc.subject.keywordAuthor | Streptococcus pneumoniae | - |
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