3g3z | pdb_00003g3z

The structure of NMB1585, a MarR family regulator from Neisseria meningitidis

spinqualitylabelsall models 3g3z, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3g3z is a 2 chain structure with sequence from Neisseria meningitidis serogroup B. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.1Å Ligands: MSE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q9JYH5_NEIMB 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 structure of the MarR-family transcription factor NMB1585 from Neisseria meningitidis has been solved using data extending to a resolution of 2.1 A. Overall, the dimeric structure resembles those of other MarR proteins, with each subunit comprising a winged helix-turn-helix (wHtH) domain connected to an alpha-helical dimerization domain. The spacing of the recognition helices of the wHtH domain indicates that NMB1585 is pre-configured for DNA binding, with a putative inducer pocket that is largely occluded by the side chains of two aromatic residues (Tyr29 and Trp53). NMB1585 was shown to bind to its own promoter region in a gel-shift assay, indicating that the protein acts as an auto-repressor. The structure of NMB1585, a MarR-family regulator from Neisseria meningitidis.,Nichols CE, Sainsbury S, Ren J, Walter TS, Verma A, Stammers DK, Saunders NJ, Owens RJ Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Mar 1;65(Pt, 3):204-9. Epub 2009 Feb 26. PMID:19255465 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Transcriptional activator 3D structures

Proteopedia Page Contributors and Editors (what is this?)

OCA