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  • Title: The crystal structure of Escherichia coli MoeA, a protein from the molybdopterin synthesis pathway.
    Author: Schrag JD, Huang W, Sivaraman J, Smith C, Plamondon J, Larocque R, Matte A, Cygler M.
    Journal: J Mol Biol; 2001 Jul 06; 310(2):419-31. PubMed ID: 11428898.
    Abstract:
    MoeA is involved in synthesis of the molybdopterin cofactor, although its function is not yet clearly defined. The three-dimensional structure of the Escherichia coli protein was solved at 2.2 A resolution. The locations of highly conserved residues among the prokaryotic and eukaryotic MoeA homologs identifies a cleft in the dimer interface as the likely functional site. Of the four domains of MoeA, domain 2 displays a novel fold and domains 1 and 4 each have only one known structural homolog. Domain 3, in contrast, is structurally similar to many other proteins. The protein that resembles domain 3 most closely is MogA, another protein required for molybdopterin cofactor synthesis. The overall similarity between MoeA and MogA, and the similarities in a constellation of residues that are strongly conserved in MoeA, suggests that these proteins bind similar ligands or substrates and may have similar functions.
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