Structure of the effector-binding domain of the LysR-type transcription factor RovM from Yersinia pseudotuberculosis.
dc.contributor.author | Quade, Nick | |
dc.contributor.author | Dieckmann, Marieke | |
dc.contributor.author | Haffke, Matthias | |
dc.contributor.author | Heroven, Ann Kathrin | |
dc.contributor.author | Dersch, Petra | |
dc.contributor.author | Heinz, Dirk W | |
dc.date.accessioned | 2011-08-26T14:30:15Z | |
dc.date.available | 2011-08-26T14:30:15Z | |
dc.date.issued | 2011-02 | |
dc.identifier.citation | Structure 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.issn | 1399-0047 | |
dc.identifier.pmid | 21245528 | |
dc.identifier.doi | 10.1107/S0907444910049681 | |
dc.identifier.uri | http://hdl.handle.net/10033/140869 | |
dc.description.abstract | In 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.iso | en | en |
dc.subject.mesh | Bacterial Proteins | en |
dc.subject.mesh | Crystallography, X-Ray | en |
dc.subject.mesh | Ligands | en |
dc.subject.mesh | Models, Molecular | en |
dc.subject.mesh | Protein Structure, Quaternary | en |
dc.subject.mesh | Protein Structure, Tertiary | en |
dc.subject.mesh | Transcription Factors | en |
dc.subject.mesh | Yersinia pseudotuberculosis | en |
dc.title | Structure of the effector-binding domain of the LysR-type transcription factor RovM from Yersinia pseudotuberculosis. | en |
dc.type | Article | en |
dc.contributor.department | Department of Molecular Structural Biology, Helmholtz Centre for Infection Research, D-38124 Braunschweig, Germany. | en |
dc.identifier.journal | Acta crystallographica. Section D, Biological crystallography | en |
refterms.dateFOA | 2018-06-13T14:17:03Z | |
html.description.abstract | In 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. |