1di7
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1.60 ANGSTROM CRYSTAL STRUCTURE OF THE MOLYBDENUM COFACTOR BIOSYNTHESIS PROTEIN MOGA FROM ESCHERICHIA COLI
OverviewOverview
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.
About this StructureAbout this Structure
1DI7 is a Single protein structure of sequence from Escherichia coli with SO4 as ligand. Full crystallographic information is available from OCA.
ReferenceReference
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
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