Structural highlights
Function
[OMPR_ECOLI] The N-terminus of this protein is required for the transcriptional expression of both major outer membrane protein genes ompF and ompC; its C-terminal moiety mediates the multimerization of the OmpR protein. As a multimer, it turns on the expression of the ompC gene; as a monomer, it turns on the expression of the ompF gene.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The C-terminal DNA-binding domain of OmpR, a positive regulator involved in osmoregulation expression of the ompF and ompC genes in Escherichia coli, has a helix-turn-helix variant motif. The 'turn' region, consisting of 11 residues, forms an RNA polymerase contact site.
Escherichia coli positive regulator OmpR has a large loop structure at the putative RNA polymerase interaction site.,Kondo H, Nakagawa A, Nishihira J, Nishimura Y, Mizuno T, Tanaka I Nat Struct Biol. 1997 Jan;4(1):28-31. PMID:8989318[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kondo H, Nakagawa A, Nishihira J, Nishimura Y, Mizuno T, Tanaka I. Escherichia coli positive regulator OmpR has a large loop structure at the putative RNA polymerase interaction site. Nat Struct Biol. 1997 Jan;4(1):28-31. PMID:8989318
