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-Structure paper
タイトル | A 3.3 Å-Resolution Structure of Hyperthermophilic Respiratory Complex III Reveals the Mechanism of Its Thermal Stability. |
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ジャーナル・号・ページ | Angew Chem Int Ed Engl, Vol. 59, Issue 1, Page 343-351, Year 2020 |
掲載日 | 2020年1月2日 |
著者 | Guoliang Zhu / Hui Zeng / Shuangbo Zhang / Jana Juli / Xiaoyun Pang / Jan Hoffmann / Yan Zhang / Nina Morgner / Yun Zhu / Guohong Peng / Hartmut Michel / Fei Sun / |
PubMed 要旨 | Respiratory chain complexes convert energy by coupling electron flow to transmembrane proton translocation. Owing to a lack of atomic structures of cytochrome bc complex (Complex III) from ...Respiratory chain complexes convert energy by coupling electron flow to transmembrane proton translocation. Owing to a lack of atomic structures of cytochrome bc complex (Complex III) from thermophilic bacteria, little is known about the adaptations of this macromolecular machine to hyperthermophilic environments. In this study, we purified the cytochrome bc complex of Aquifex aeolicus, one of the most extreme thermophilic bacteria known, and determined its structure with and without an inhibitor at 3.3 Å resolution. Several residues unique for thermophilic bacteria were detected that provide additional stabilization for the structure. An extra transmembrane helix at the N-terminus of cyt. c was found to greatly enhance the interaction between cyt. b and cyt. c , and to bind a phospholipid molecule to stabilize the complex in the membrane. These results provide the structural basis for the hyperstability of the cytochrome bc complex in an extreme thermal environment. |
リンク | Angew Chem Int Ed Engl / PubMed:31778296 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.2 - 3.3 Å |
構造データ | |
化合物 | ChemComp-FES: ChemComp-HEM: ChemComp-DLX: ChemComp-PGV: ChemComp-HEC: ChemComp-AMY: |
由来 |
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キーワード | OXIDOREDUCTASE / Respiratory chain / Complex III / Hyperthermophilic mechanism / antimycin A |