1JMZ

crystal structure of a quinohemoprotein amine dehydrogenase from pseudomonas putida with inhibitor

1JMZ の概要

• エントリーDOI: 10.2210/pdb1jmz/pdb
• 関連するPDBエントリー: 1JMX
• 分子名称: Amine Dehydrogenase, NICKEL (II) ION, HEME C, ... (7 entities in total)
• 機能のキーワード: amine dehydrogenase, oxidoreductase
• 由来する生物種: Pseudomonas putida; 詳細
• 細胞内の位置: Periplasm: P0A182
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 103350.71

構造登録者

Satoh, A.,Miyahara, I.,Hirotsu, K. (登録日: 2001-07-20, 公開日: 2002-01-16, 最終更新日: 2025-03-26)

主引用文献

Satoh, A.,Kim, J.K.,Miyahara, I.,Devreese, B.,Vandenberghe, I.,Hacisalihoglu, A.,Okajima, T.,Kuroda, S.,Adachi, O.,Duine, J.A.,Van Beeumen, J.,Tanizawa, K.,Hirotsu, K.
Crystal structure of quinohemoprotein amine dehydrogenase from Pseudomonas putida. Identification of a novel quinone cofactor encaged by multiple thioether cross-bridges.
J.Biol.Chem., 277:2830-2834, 2002

PubMed Abstract: The crystal structure of a quinohemoprotein amine dehydrogenase from Pseudomonas putida has been determined at 1.9-A resolution. The enzyme comprises three non-identical subunits: a four-domain alpha-subunit that harbors a di-heme cytochrome c, a seven-bladed beta-propeller beta-subunit that provides part of the active site, and a small gamma-subunit that contains a novel cross-linked, proteinous quinone cofactor, cysteine tryptophylquinone. More surprisingly, the catalytic gamma-subunit contains three additional chemical cross-links that encage the cysteine tryptophylquinone cofactor, involving a cysteine side chain bridged to either an Asp or Glu residue all in a hitherto unknown thioether bonding with a methylene carbon atom of acidic amino acid side chains. Thus, the structure of the 79-residue gamma-subunit is quite unusual, containing four internal cross-links in such a short polypeptide chain that would otherwise be difficult to fold into a globular structure.

PubMed: 11704672
DOI: 10.1074/jbc.M109090200

実験手法

X-RAY DIFFRACTION (2 Å)