Crystal structure of the VanR transcription factor and the role of its unique -helix in effector recognition
DC Field | Value | Language |
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dc.contributor.author | Kwak, Yun Mi | - |
dc.contributor.author | Park, Sun Cheol | - |
dc.contributor.author | Na, Hye-won | - |
dc.contributor.author | Kang, Seung Goo | - |
dc.contributor.author | Lee, Geun-Shik | - |
dc.contributor.author | Ko, Hyun-Jeong | - |
dc.contributor.author | Kim, Pyeung-Hyeun | - |
dc.contributor.author | Oh, Byung-Chul | - |
dc.contributor.author | Yoon, Sung-il | - |
dc.date.available | 2020-02-27T09:41:10Z | - |
dc.date.created | 2020-02-06 | - |
dc.date.issued | 2018-10 | - |
dc.identifier.issn | 1742-464X | - |
dc.identifier.uri | https://scholarworks.bwise.kr/gachon/handle/2020.sw.gachon/3292 | - |
dc.description.abstract | VanR is a negative transcriptional regulator of bacteria that belongs to the PadR family and modulates the expression of vanillate transport and degradation proteins in response to vanillate. Although VanR plays a key role in the utilization of vanillate as a carbon source, it is barely understood how VanR recognizes its effector. Thus, our knowledge concerning the gene regulatory mechanism of VanR is limited. Here, we reveal the vanillate-binding mode of VanR through structural, biophysical, and mutational studies. Similar to other PadR family members, VanR forms a functional dimer, and each VanR subunit consists of an N-terminal DNA-binding domain (NTD) and a C-terminal dimerization domain (CTD). One VanR dimer simultaneously binds two vanillate molecules using two interdomain cavities, as observed in PadR. In contrast to these common features, VanR contains an additional -helix, i, that has not been found in other PadR family members. The i helix functions as an interdomain crosslinker that mediates interactions between the NTD and the CTD. In addition, the VanR-specific i helix plays a key role in the formation of a unique effector-binding site. As a result, the effector-binding mode of VanR is distinguishable from that of PadR in the location and accessibility of the effector-binding site as well as the orientation of its bound effector. Furthermore, we propose the DNA-binding mode and vanillate-mediated transcriptional regulation mechanism of VanR based on comparative structural and mutational analyses. DatabasesThe atomic coordinates and the structure factors for VanR (PDB ID ) have been deposited in the Protein Data Bank, . | - |
dc.language | 영어 | - |
dc.language.iso | en | - |
dc.publisher | WILEY | - |
dc.relation.isPartOf | FEBS JOURNAL | - |
dc.subject | PHENOLIC-ACID DECARBOXYLASE | - |
dc.subject | P-COUMARATE DECARBOXYLASE | - |
dc.subject | CORYNEBACTERIUM-GLUTAMICUM | - |
dc.subject | LACTOBACILLUS-PLANTARUM | - |
dc.subject | BACILLUS-SUBTILIS | - |
dc.subject | STRESS-RESPONSE | - |
dc.subject | PADR | - |
dc.subject | REGULATOR | - |
dc.subject | REPRESSOR | - |
dc.subject | METABOLISM | - |
dc.title | Crystal structure of the VanR transcription factor and the role of its unique -helix in effector recognition | - |
dc.type | Article | - |
dc.type.rims | ART | - |
dc.description.journalClass | 1 | - |
dc.identifier.wosid | 000447880900009 | - |
dc.identifier.doi | 10.1111/febs.14629 | - |
dc.identifier.bibliographicCitation | FEBS JOURNAL, v.285, no.20, pp.3786 - 3800 | - |
dc.identifier.scopusid | 2-s2.0-85052454896 | - |
dc.citation.endPage | 3800 | - |
dc.citation.startPage | 3786 | - |
dc.citation.title | FEBS JOURNAL | - |
dc.citation.volume | 285 | - |
dc.citation.number | 20 | - |
dc.contributor.affiliatedAuthor | Oh, Byung-Chul | - |
dc.type.docType | Article | - |
dc.subject.keywordAuthor | crystal structure | - |
dc.subject.keywordAuthor | effector recognition | - |
dc.subject.keywordAuthor | transcription factor | - |
dc.subject.keywordAuthor | vanillate | - |
dc.subject.keywordAuthor | VanR | - |
dc.subject.keywordPlus | PHENOLIC-ACID DECARBOXYLASE | - |
dc.subject.keywordPlus | P-COUMARATE DECARBOXYLASE | - |
dc.subject.keywordPlus | CORYNEBACTERIUM-GLUTAMICUM | - |
dc.subject.keywordPlus | LACTOBACILLUS-PLANTARUM | - |
dc.subject.keywordPlus | BACILLUS-SUBTILIS | - |
dc.subject.keywordPlus | STRESS-RESPONSE | - |
dc.subject.keywordPlus | PADR | - |
dc.subject.keywordPlus | REGULATOR | - |
dc.subject.keywordPlus | REPRESSOR | - |
dc.subject.keywordPlus | METABOLISM | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
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