Structure of the effector-binding domain of the LysR-type transcription factor RovM from Yersinia pseudotuberculosis.
Cast your vote
You can rate an item by clicking the amount of stars they wish to award to this item.
When enough users have cast their vote on this item, the average rating will also be shown.
Your vote was cast
Thank you for your feedback
Thank you for your feedback
MetadataShow full item record
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.
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.
AffiliationDepartment of Molecular Structural Biology, Helmholtz Centre for Infection Research, D-38124 Braunschweig, Germany.
The following license files are associated with this item:
- RovM, a novel LysR-type regulator of the virulence activator gene rovA, controls cell invasion, virulence and motility of Yersinia pseudotuberculosis.
- Authors: Heroven AK, Dersch P
- Issue date: 2006 Dec
- Full-length structures of BenM and two variants reveal different oligomerization schemes for LysR-type transcriptional regulators.
- Authors: Ruangprasert A, Craven SH, Neidle EL, Momany C
- Issue date: 2010 Dec 10
- Crystal structure of a full-length LysR-type transcriptional regulator, CbnR: unusual combination of two subunit forms and molecular bases for causing and changing DNA bend.
- Authors: Muraoka S, Okumura R, Ogawa N, Nonaka T, Miyashita K, Senda T
- Issue date: 2003 May 2
- Crystal structure of ArgP from Mycobacterium tuberculosis confirms two distinct conformations of full-length LysR transcriptional regulators and reveals its function in DNA binding and transcriptional regulation.
- Authors: Zhou X, Lou Z, Fu S, Yang A, Shen H, Li Z, Feng Y, Bartlam M, Wang H, Rao Z
- Issue date: 2010 Mar 5
- A Csr-type regulatory system, including small non-coding RNAs, regulates the global virulence regulator RovA of Yersinia pseudotuberculosis through RovM.
- Authors: Heroven AK, Böhme K, Rohde M, Dersch P
- Issue date: 2008 Jun