1di6

1.45 A CRYSTAL STRUCTURE OF THE MOLYBDENUMM COFACTOR BIOSYNTHESIS PROTEIN MOGA FROM ESCHERICHIA COLI

spinqualitylabelsall models 1di6, resolution 1.45Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1di6 is a 1 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: SO4 Resources: FirstGlance, OCA, RCSB, PDBsum Function [MOG_ECOLI] Catalyzes the adenylation of molybdopterin as part of the biosynthesis of the molybdenum-cofactor. 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 Molybdenum cofactor (Moco) biosynthesis is an evolutionarily conserved pathway in archaea, eubacteria, and eukaryotes, including humans. Genetic deficiencies of enzymes involved in this biosynthetic pathway trigger an autosomal recessive disease with severe neurological symptoms, which usually leads to death in early childhood. The MogA protein exhibits affinity for molybdopterin, the organic component of Moco, and has been proposed to act as a molybdochelatase incorporating molybdenum into Moco. MogA is related to the protein gephyrin, which, in addition to its role in Moco biosynthesis, is also responsible for anchoring glycinergic receptors to the cytoskeleton at inhibitory synapses. The high resolution crystal structure of the Escherichia coli MogA protein has been determined, and it reveals a trimeric arrangement in which each monomer contains a central, mostly parallel beta-sheet surrounded by alpha-helices on either side. Based on structural and biochemical data, a putative active site was identified, including two residues that are essential for the catalytic mechanism. Crystal structure of the gephyrin-related molybdenum cofactor biosynthesis protein MogA from Escherichia coli.,Liu MT, Wuebbens MM, Rajagopalan KV, Schindelin H J Biol Chem. 2000 Jan 21;275(3):1814-22. PMID:10636880 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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