3onm

Publication Abstract from PubMed

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 A. 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.

Structure of the effector-binding domain of the LysR-type transcription factor RovM from Yersinia pseudotuberculosis.,Quade N, Dieckmann M, Haffke M, Heroven AK, Dersch P, Heinz DW Acta Crystallogr D Biol Crystallogr. 2011 Feb;67(Pt 2):81-90. Epub 2011, Jan 8. PMID:21245528^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.