3EH5
Structure of the reduced form of cytochrome ba3 oxidase from Thermus thermophilus
3EH5 の概要
| エントリーDOI | 10.2210/pdb3eh5/pdb |
| 関連するPDBエントリー | 1XME 2qpd 2qpe 3EH3 3EH4 |
| 分子名称 | Cytochrome c oxidase subunit 1, Cytochrome c oxidase subunit 2, Cytochrome c oxidase polypeptide 2A, ... (9 entities in total) |
| 機能のキーワード | cytochrome ba3 oxidase, heme, integral membrane protein, copper, electron transport, hydrogen ion transport, ion transport, iron, metal-binding, oxidoreductase, respiratory chain, transmembrane, transport, formylation, cell membrane, membrane |
| 由来する生物種 | Thermus thermophilus 詳細 |
| タンパク質・核酸の鎖数 | 3 |
| 化学式量合計 | 93929.51 |
| 構造登録者 | Liu, B.,Chen, Y.,Doukov, T.,Soltis, S.M.,Stout, D.,Fee, J.A. (登録日: 2008-09-11, 公開日: 2009-04-21, 最終更新日: 2023-08-30) |
| 主引用文献 | Liu, B.,Chen, Y.,Doukov, T.,Soltis, S.M.,Stout, C.D.,Fee, J.A. Combined microspectrophotometric and crystallographic examination of chemically reduced and X-ray radiation-reduced forms of cytochrome ba3 oxidase from Thermus thermophilus: structure of the reduced form of the enzyme. Biochemistry, 48:820-826, 2009 Cited by PubMed Abstract: Three paths for obtaining crystals of reduced (II-E4Q/I-K258R) cytochrome ba(3) are described, and the structures of these are reported at approximately 2.8-3.0 A resolution. Microspectrophotometry of single crystals of Thermus ba(3) oxidase at 100 K was used to show that crystals of the oxidized enzyme are reduced in an intense X-ray (beam line 7-1 at the Stanford Synchrotron Radiation Laboratory), being nearly complete in 1 min. The previously reported structures of ba(3) (Protein Data Bank entries 1EHK and 1XME ), having a crystallographically detectable water between the Cu(B) and Fe(a3) metals of the dinuclear center, actually represent the X-ray radiation-reduced enzyme. Dithionite-reduced crystals or crystals formed from dithionite-reduced enzyme revealed the absence of the above-mentioned water and an increase in the Cu(B)-Fe(a3) distance of approximately 0.3 A. The new structures are discussed in terms of enzyme function. An unexpected optical absorption envelope at approximately 590 nm is also reported. This spectral feature is tentatively thought to arise from a five-coordinate, low-spin, ferrous heme a(3) that is trapped in the frozen crystals. PubMed: 19140675DOI: 10.1021/bi801759a 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.8 Å) |
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