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1Q0D

Crystal structure of Ni-containing superoxide dismutase with Ni-ligation corresponding to the oxidized state

1Q0D の概要
エントリーDOI10.2210/pdb1q0d/pdb
関連するPDBエントリー1Q0F 1Q0G 1Q0K 1Q0M
分子名称Superoxide dismutase [Ni], SULFATE ION, NICKEL (III) ION, ... (4 entities in total)
機能のキーワードhomohexamer of four-helix bundles, oxidoreductase
由来する生物種Streptomyces seoulensis
細胞内の位置Cytoplasm: P80734
タンパク質・核酸の鎖数12
化学式量合計160736.70
構造登録者
Wuerges, J.,Lee, J.-W.,Yim, Y.-I.,Yim, H.-S.,Kang, S.-O.,Djinovic Carugo, K. (登録日: 2003-07-16, 公開日: 2004-05-18, 最終更新日: 2024-02-14)
主引用文献Wuerges, J.,Lee, J.-W.,Yim, Y.-I.,Yim, H.-S.,Kang, S.-O.,Djinovic Carugo, K.
Crystal structure of nickel-containing superoxide dismutase reveals another type of active site
Proc.Natl.Acad.Sci.USA, 101:8569-8574, 2004
Cited by
PubMed Abstract: Superoxide dismutases (SODs, EC 1.15.1.1) are ubiquitous enzymes that efficiently catalyze the dismutation of superoxide radical anions to protect biological molecules from oxidative damage. The crystal structure of nickel-containing SOD (NiSOD) from Streptomyces seoulensis was determined for the resting, x-ray-reduced, and thiosulfate-reduced enzyme state. NiSOD is a homohexamer consisting of four-helix-bundle subunits. The catalytic center resides in the N-terminal active-site loop, where a Ni(III) ion is coordinated by the amino group of His-1, the amide group of Cys-2, two thiolate groups of Cys-2 and Cys-6, and the imidazolate of His-1 as axial ligand that is lost in the chemically reduced state as well as after x-ray-induced reduction. This structure represents a third class of SODs concerning the catalytic metal species, subunit structure, and oligomeric organization. It adds a member to the small number of Ni-metalloenzymes and contributes with its Ni(III) active site to the general understanding of Ni-related biochemistry. NiSOD is shown to occur also in bacteria other than Streptomyces and is predicted to be present in some cyanobacteria.
PubMed: 15173586
DOI: 10.1073/pnas.0308514101
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 1q0d
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2025-12-31に公開中

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