Structural and Biochemical Analysis of the Citrate-Responsive Mechanism of the Regulatory Domain of Catabolite Control Protein E from Staphylococcus aureus
DC Field | Value | Language |
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dc.contributor.author | Chen, Jinli | - |
dc.contributor.author | Shang, Fei | - |
dc.contributor.author | Wang, Lulu | - |
dc.contributor.author | Zou, Linhai | - |
dc.contributor.author | Bu, Tingting | - |
dc.contributor.author | Jin, Liming | - |
dc.contributor.author | Dong, Yuesheng | - |
dc.contributor.author | Ha, Nam-Chul | - |
dc.contributor.author | Quan, Chunshan | - |
dc.contributor.author | Nam, Ki Hyun | - |
dc.contributor.author | Xu, Yongbin | - |
dc.date.accessioned | 2021-09-02T05:03:16Z | - |
dc.date.available | 2021-09-02T05:03:16Z | - |
dc.date.created | 2021-06-19 | - |
dc.date.issued | 2018-10-23 | - |
dc.identifier.issn | 0006-2960 | - |
dc.identifier.uri | https://scholar.korea.ac.kr/handle/2021.sw.korea/72449 | - |
dc.description.abstract | Catabolite control protein E (CcpE) is a LysR-type transcriptional regulator that positively regulates the transcription of the first two enzymes of the TCA cycle, namely, citZ and citB, by sensing accumulated intracellular citrate. CcpE comprises an N-terminal DNA-binding domain and a C-terminal regulatory domain (RD) and senses citrate with conserved arginine residues in the RD. Although the crystal structure of the apo SaCcpE-RD has been reported, the citrate-responsive and DNA-binding mechanisms by which CcpE regulates TCA activity remain unclear. Here, we report the crystal structure of the apo and citrate-bound SaCcpE-RDs. The SaCcpE-RD exhibits conformational changes between the two subdomains via hinge motion of the central beta 4 and beta 10 strands. The citrate molecule is located in a positively charged cavity between the two subdomains and interacts with the highly conserved Ser98, Leu100, Arg145, and Arg256 residues. Compared with that of the apo SaCcpE-RD, the distance between the two subdomains of the citrate-bound SaCcpE-RD is more than similar to 3 angstrom due to the binding of the citrate molecule, and this form exhibits a closed structure. The SaCcpE-RD exhibits various citrate-binding-independent conformational changes at the contacting interface. The SaCcpE-RD prefers the dimeric state in solution, whereas the SaCcpE-FL prefers the tetrameric state. Our results provide insight into the molecular function of SaCcpE. | - |
dc.language | English | - |
dc.language.iso | en | - |
dc.publisher | AMER CHEMICAL SOC | - |
dc.subject | VIRULENCE DETERMINANT PRODUCTION | - |
dc.subject | TRANSCRIPTIONAL REGULATOR | - |
dc.subject | E CCPE | - |
dc.subject | GENE | - |
dc.subject | REPRESSION | - |
dc.title | Structural and Biochemical Analysis of the Citrate-Responsive Mechanism of the Regulatory Domain of Catabolite Control Protein E from Staphylococcus aureus | - |
dc.type | Article | - |
dc.contributor.affiliatedAuthor | Nam, Ki Hyun | - |
dc.identifier.doi | 10.1021/acs.biochem.8b00671 | - |
dc.identifier.scopusid | 2-s2.0-85054603586 | - |
dc.identifier.wosid | 000448752500003 | - |
dc.identifier.bibliographicCitation | BIOCHEMISTRY, v.57, no.42, pp.6054 - 6060 | - |
dc.relation.isPartOf | BIOCHEMISTRY | - |
dc.citation.title | BIOCHEMISTRY | - |
dc.citation.volume | 57 | - |
dc.citation.number | 42 | - |
dc.citation.startPage | 6054 | - |
dc.citation.endPage | 6060 | - |
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.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.subject.keywordPlus | VIRULENCE DETERMINANT PRODUCTION | - |
dc.subject.keywordPlus | TRANSCRIPTIONAL REGULATOR | - |
dc.subject.keywordPlus | E CCPE | - |
dc.subject.keywordPlus | GENE | - |
dc.subject.keywordPlus | REPRESSION | - |
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