1odd | pdb_00001odd

OMPR C-TERMINAL DOMAIN (OMPR-C) FROM ESCHERICHIA COLI

spinqualitylabelsall models 1odd, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1odd is a 1 chain structure with sequence from Ecoli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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