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1FC5

CRYSTAL STRUCTURE OF MOLYBDOPTERIN BIOSYNTHESIS MOEA PROTEIN

1FC5 の概要
エントリーDOI10.2210/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: 11428898
DOI: 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)
構造検証レポート
Validation report summary of 1fc5
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-07-09に公開中

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