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dc.contributor.authorQuade, Nick
dc.contributor.authorDieckmann, Marieke
dc.contributor.authorHaffke, Matthias
dc.contributor.authorHeroven, Ann Kathrin
dc.contributor.authorDersch, Petra
dc.contributor.authorHeinz, Dirk W
dc.date.accessioned2011-08-26T14:30:15Z
dc.date.available2011-08-26T14:30:15Z
dc.date.issued2011-02
dc.identifier.citationStructure of the effector-binding domain of the LysR-type transcription factor RovM from Yersinia pseudotuberculosis. 2011, 67 (Pt 2):81-90 Acta Crystallogr. D Biol. Crystallogr.en
dc.identifier.issn1399-0047
dc.identifier.pmid21245528
dc.identifier.doi10.1107/S0907444910049681
dc.identifier.urihttp://hdl.handle.net/10033/140869
dc.description.abstractIn enteropathogenic Yersinia, the expression of several early-phase virulence factors such as invasin is tightly regulated in response to environmental cues. The responsible regulatory network is complex, involving several regulatory RNAs and proteins such as the LysR-type transcription regulator (LTTR) RovM. In this study, the crystal structure of the effector-binding domain (EBD) of RovM, the first LTTR protein described as being involved in virulence regulation, was determined at a resolution of 2.4 Å. Size-exclusion chromatography and comparison with structures of full-length LTTRs show that RovM is most likely to adopt a tetrameric arrangement with two distant DNA-binding domains (DBDs), causing the DNA to bend around it. Additionally, a cavity was detected in RovM which could bind small inducer molecules.
dc.language.isoenen
dc.subject.meshBacterial Proteinsen
dc.subject.meshCrystallography, X-Rayen
dc.subject.meshLigandsen
dc.subject.meshModels, Molecularen
dc.subject.meshProtein Structure, Quaternaryen
dc.subject.meshProtein Structure, Tertiaryen
dc.subject.meshTranscription Factorsen
dc.subject.meshYersinia pseudotuberculosisen
dc.titleStructure of the effector-binding domain of the LysR-type transcription factor RovM from Yersinia pseudotuberculosis.en
dc.typeArticleen
dc.contributor.departmentDepartment of Molecular Structural Biology, Helmholtz Centre for Infection Research, D-38124 Braunschweig, Germany.en
dc.identifier.journalActa crystallographica. Section D, Biological crystallographyen
refterms.dateFOA2018-06-13T14:17:03Z
html.description.abstractIn enteropathogenic Yersinia, the expression of several early-phase virulence factors such as invasin is tightly regulated in response to environmental cues. The responsible regulatory network is complex, involving several regulatory RNAs and proteins such as the LysR-type transcription regulator (LTTR) RovM. In this study, the crystal structure of the effector-binding domain (EBD) of RovM, the first LTTR protein described as being involved in virulence regulation, was determined at a resolution of 2.4 Å. Size-exclusion chromatography and comparison with structures of full-length LTTRs show that RovM is most likely to adopt a tetrameric arrangement with two distant DNA-binding domains (DBDs), causing the DNA to bend around it. Additionally, a cavity was detected in RovM which could bind small inducer molecules.


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