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Crystal structure of the EnvZ periplasmic domain with CHAPS

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dc.contributor.authorHwang, Eunha-
dc.contributor.authorCheong, Hae-Kap-
dc.contributor.authorKim, Sang-Yoon-
dc.contributor.authorKwon, Ohsuk-
dc.contributor.authorBlain, Katherine Y.-
dc.contributor.authorChoe, Senyon-
dc.contributor.authorYeo, Kwon Joo-
dc.contributor.authorJung, Yong Woo-
dc.contributor.authorJeon, Young Ho-
dc.contributor.authorCheong, Chaejoon-
dc.date.accessioned2021-09-03T06:45:18Z-
dc.date.available2021-09-03T06:45:18Z-
dc.date.created2021-06-16-
dc.date.issued2017-05-
dc.identifier.issn0014-5793-
dc.identifier.urihttps://scholar.korea.ac.kr/handle/2021.sw.korea/83612-
dc.description.abstractBacteria sense and respond to osmolarity through the EnvZ-OmpR two-component system. The structure of the periplasmic sensor domain of EnvZ (EnvZ-PD) is not available yet. Here, we present the crystal structure of EnvZ-PD in the presence of CHAPS detergent. The structure of EnvZ-PD shows similar folding topology to the PDC domains of PhoQ, DcuS, and CitA, but distinct orientations of helices and beta-hairpin structures. The CD and NMR spectra of EnvZ-PD in the presence of cholate, a major component of bile salts, are similar to those with CHAPS. Chemical cross-linking shows that the dimerization of EnvZ-PD is significantly inhibited by the CHAPS and cholate. Together with beta-galactosidase assay, these results suggest that bile salts may affect the EnvZ structure and function in Escherichia coli.-
dc.languageEnglish-
dc.language.isoen-
dc.publisherWILEY-
dc.subjectTRANSMEMBRANE SIGNAL-TRANSDUCTION-
dc.subjectHISTIDINE KINASE ENVZ-
dc.subjectPORIN GENE-EXPRESSION-
dc.subjectESCHERICHIA-COLI-
dc.subjectSENSOR-
dc.subjectOMPR-
dc.subjectBACTERIAL-
dc.subjectFLUORESCENCE-
dc.subjectTRANSITIONS-
dc.subjectPROTEIN-
dc.titleCrystal structure of the EnvZ periplasmic domain with CHAPS-
dc.typeArticle-
dc.contributor.affiliatedAuthorYeo, Kwon Joo-
dc.contributor.affiliatedAuthorJung, Yong Woo-
dc.contributor.affiliatedAuthorJeon, Young Ho-
dc.identifier.doi10.1002/1873-3468.12658-
dc.identifier.scopusid2-s2.0-85019105528-
dc.identifier.wosid000403353700009-
dc.identifier.bibliographicCitationFEBS LETTERS, v.591, no.10, pp.1419 - 1428-
dc.relation.isPartOfFEBS LETTERS-
dc.citation.titleFEBS LETTERS-
dc.citation.volume591-
dc.citation.number10-
dc.citation.startPage1419-
dc.citation.endPage1428-
dc.type.rimsART-
dc.type.docTypeArticle-
dc.description.journalClass1-
dc.description.journalRegisteredClassscie-
dc.description.journalRegisteredClassscopus-
dc.relation.journalResearchAreaBiochemistry & Molecular Biology-
dc.relation.journalResearchAreaBiophysics-
dc.relation.journalResearchAreaCell Biology-
dc.relation.journalWebOfScienceCategoryBiochemistry & Molecular Biology-
dc.relation.journalWebOfScienceCategoryBiophysics-
dc.relation.journalWebOfScienceCategoryCell Biology-
dc.subject.keywordPlusTRANSMEMBRANE SIGNAL-TRANSDUCTION-
dc.subject.keywordPlusHISTIDINE KINASE ENVZ-
dc.subject.keywordPlusPORIN GENE-EXPRESSION-
dc.subject.keywordPlusESCHERICHIA-COLI-
dc.subject.keywordPlusSENSOR-
dc.subject.keywordPlusOMPR-
dc.subject.keywordPlusBACTERIAL-
dc.subject.keywordPlusFLUORESCENCE-
dc.subject.keywordPlusTRANSITIONS-
dc.subject.keywordPlusPROTEIN-
dc.subject.keywordAuthorEnvZ-
dc.subject.keywordAuthorperiplasmic domain-
dc.subject.keywordAuthorX-ray crystallography-
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