title: The crystal structure of Escherichia coli MoeA, a protein from the molybdopterin synthesis pathway.
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.
authors: Biotechnology Research Institute, National Research Council of Canada, 6100 Royalmount Avenue, Montreal, PQ, Canada. joe@bri.nrc.ca
authors: J D
authors: JD
authors: Schrag
authors: W
authors: W
authors: Huang
authors: J
authors: J
authors: Sivaraman
authors: C
authors: C
authors: Smith
authors: J
authors: J
authors: Plamondon
authors: R
authors: R
authors: Larocque
authors: A
authors: A
authors: Matte
authors: M
authors: M
authors: Cygler
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism; D001665:Binding Sites; D003067:Coenzymes / Q000096:biosynthesis* / Q000737:chemistry / Q000378:metabolism; D017124:Conserved Sequence; D018360:Crystallography, X-Ray; D019281:Dimerization; D004926:Escherichia coli / Q000201:enzymology*; D029968:Escherichia coli Proteins; D008027:Light; D008667:Metalloproteins / Q000096:biosynthesis* / Q000737:chemistry / Q000378:metabolism; D008958:Models, Molecular; D008969:Molecular Sequence Data; D000090006:Molybdenum Cofactors; D020836:Protein Structure, Quaternary; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011621:Pteridines / Q000737:chemistry / Q000378:metabolism; D012542:Scattering, Radiation; D016415:Sequence Alignment; D013466:Sulfurtransferases / Q000737:chemistry* / Q000378:metabolism*
chemical_list: D001426:Bacterial Proteins; D003067:Coenzymes; D029968:Escherichia coli Proteins; D008667:Metalloproteins; D000090006:Molybdenum Cofactors; D011621:Pteridines; D013466:Sulfurtransferases; C404104:Mog protein, E coli; C022261:molybdopterin; C111302:MoeA protein, E coli