Structure of the effector-binding domain of the LysR-type transcription factor RovM from Yersinia pseudotuberculosis.
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.
Department of Molecular Structural Biology, Helmholtz Centre for Infection Research, D-38124 Braunschweig, Germany.
Nick
N
Quade
Marieke
M
Dieckmann
Matthias
M
Haffke
Ann Kathrin
AK
Heroven
Petra
P
Dersch
Dirk W
DW
Heinz
D001426:Bacterial Proteins / Q000737:chemistry*; D018360:Crystallography, X-Ray; D008024:Ligands; D008958:Models, Molecular; D020836:Protein Structure, Quaternary; D017434:Protein Structure, Tertiary; D014157:Transcription Factors / Q000737:chemistry*; D015011:Yersinia pseudotuberculosis / Q000737:chemistry*
D001426:Bacterial Proteins; D008024:Ligands; D014157:Transcription Factors; C073470:LysR protein, Bacteria