1FC5
CRYSTAL STRUCTURE OF MOLYBDOPTERIN BIOSYNTHESIS MOEA PROTEIN
1FC5 の概要
エントリーDOI | 10.2210/pdb1fc5/pdb |
分子名称 | MOLYBDOPTERIN BIOSYNTHESIS MOEA PROTEIN, MAGNESIUM ION (3 entities in total) |
機能のキーワード | molybdopterin, four modules, with magnesium, montreal-kingston bacterial structural genomics initiative, bsgi, structural genomics, biosynthetic protein |
由来する生物種 | Escherichia coli |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 89011.04 |
構造登録者 | Huang, W.,Cygler, M.,Montreal-Kingston Bacterial Structural Genomics Initiative (BSGI) (登録日: 2000-07-17, 公開日: 2001-07-25, 最終更新日: 2024-10-16) |
主引用文献 | Schrag, J.D.,Huang, W.,Sivaraman, J.,Smith, C.,Plamondon, J.,Larocque, R.,Matte, A.,Cygler, M. The crystal structure of Escherichia coli MoeA, a protein from the molybdopterin synthesis pathway. J.Mol.Biol., 310:419-431, 2001 Cited by PubMed 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. PubMed: 11428898DOI: 10.1006/jmbi.2001.4771 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.2 Å) |
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