1r2k | pdb_00001r2k

Crystal structure of MoaB from Escherichia coli

spinqualitylabelsall models 1r2k, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1r2k is a 2 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: SO4 NonStd Res: MSE Gene: MOAB, CHLA2, B0782, Z1001, ECS0860 ("Bacillus coli" Migula 1895) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Function [MOAB_ECOLI] May be involved in the biosynthesis of molybdopterin. Can bind GTP and has low GTPase activity. Can bind MPT, but has no MPT adenylyl transferase activity. 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 moaABC operon of Escherichia coli is involved in early steps of the biosynthesis of the molybdenum-binding cofactor molybdopterin, but the precise functions of the cognate proteins are not known. The crystal structure of the MoaB protein from E. coli was determined by multiple anomalous dispersion at 2.1 angstroms A resolution and refined to an R factor of 20.4% (Rfree = 25.0%). The protein is a 32-symmetric hexamer, with the monomers consisting of a central beta-sheet flanked by helices on both sides. The overall fold of the monomer is similar to those of the MogA protein of E. coli, the G-domains of rat and human gephyrin and the G-domains of Cnx1 protein from A. thaliana, all of which are involved in the insertion of an unknown molybdenum species into molybdopterin to form the molybdenum cofactor. Furthermore, the MoaB protein shows significant sequence similarity to the cinnamon protein from Drosophila melanogaster. In addition to other functions, all these proteins are involved in the biosynthesis of the molybdenum cofactor and have been shown to bind molybdopterin. The close structural homology to MogA and the gephyrin and Cnx1 domains suggests that MoaB may bind a hitherto unidentified pterin compound, possibly an intermediate in molybdopterin biosynthesis. Structure of the molybdenum-cofactor biosynthesis protein MoaB of Escherichia coli.,Bader G, Gomez-Ortiz M, Haussmann C, Bacher A, Huber R, Fischer M Acta Crystallogr D Biol Crystallogr. 2004 Jun;60(Pt 6):1068-75. Epub 2004, May 21. PMID:15159566 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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