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Structure of the effector-binding domain of the LysR-type transcription factor RovM from Yersinia pseudotuberculosis.
Quade, Nick Dieckmann, Marieke Haffke, Matthias Heroven, Ann Kathrin Heinz, Dirk W
Quade, Nick
Dieckmann, Marieke
Haffke, Matthias
Heroven, Ann Kathrin
Heinz, Dirk W
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2011-02
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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.
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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.
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Article
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en
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1399-0047