4PI2

Crystal structure of particulate methane monooxygenase from Methylocystis sp. ATCC 49242 (Rockwell) soaked in zinc

4PI2 の概要

• エントリーDOI: 10.2210/pdb4pi2/pdb
• 関連するPDBエントリー: 4PHZ 4PI0
• 分子名称: unknown peptide, Particulate methane monooxygenase subunit A, Particulate methane monooxygenase subunit B, ... (7 entities in total)
• 機能のキーワード: bacterial proteins, binding sites, copper, zinc, methylocystaceae, oxygenases, protein binding, oxidoreductase
• 由来する生物種: Methylocystis sp. ATCC 49242; 詳細
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 317688.90

構造登録者

Sirajuddin, S.,Rosenzweig, A.C. (登録日: 2014-05-07, 公開日: 2014-06-25, 最終更新日: 2024-10-23)

主引用文献

Sirajuddin, S.,Barupala, D.,Helling, S.,Marcus, K.,Stemmler, T.L.,Rosenzweig, A.C.
Effects of zinc on particulate methane monooxygenase activity and structure.
J.Biol.Chem., 289:21782-21794, 2014

PubMed Abstract: Particulate methane monooxygenase (pMMO) is a membrane-bound metalloenzyme that oxidizes methane to methanol in methanotrophic bacteria. Zinc is a known inhibitor of pMMO, but the details of zinc binding and the mechanism of inhibition are not understood. Metal binding and activity assays on membrane-bound pMMO from Methylococcus capsulatus (Bath) reveal that zinc inhibits pMMO at two sites that are distinct from the copper active site. The 2.6 Å resolution crystal structure of Methylocystis species strain Rockwell pMMO reveals two previously undetected bound lipids, and metal soaking experiments identify likely locations for the two zinc inhibition sites. The first is the crystallographic zinc site in the pmoC subunit, and zinc binding here leads to the ordering of 10 previously unobserved residues. A second zinc site is present on the cytoplasmic side of the pmoC subunit. Parallels between these results and zinc inhibition studies of several respiratory complexes suggest that zinc might inhibit proton transfer in pMMO.

PubMed: 24942740
DOI: 10.1074/jbc.M114.581363

実験手法

X-RAY DIFFRACTION (3.33 Å)