6KLS
Hyperthermophilic respiratory Complex III
Summary for 6KLS
| Entry DOI | 10.2210/pdb6kls/pdb |
| EMDB information | 0716 |
| Descriptor | Rieske-I iron sulfur protein, cytochrome b subunit, Cytochrome c, ... (8 entities in total) |
| Functional Keywords | respiratory chain, complex iii, hyperthermophilic mechanism, oxidoreductase |
| Biological source | Aquifex aeolicus (strain VF5) More |
| Total number of polymer chains | 6 |
| Total formula weight | 198446.95 |
| Authors | Fei, S.,Hartmut, M.,Yun, Z.,Guohong, P.,Guoliang, Z.,Hui, Z.,Shuangbo, Z.,Xiaoyun, P.,Yan, Z. (deposition date: 2019-07-30, release date: 2020-05-13, Last modification date: 2025-09-17) |
| Primary citation | Zhu, G.,Zeng, H.,Zhang, S.,Juli, J.,Pang, X.,Hoffmann, J.,Zhang, Y.,Morgner, N.,Zhu, Y.,Peng, G.,Michel, H.,Sun, F. A 3.3 angstrom -Resolution Structure of Hyperthermophilic Respiratory Complex III Reveals the Mechanism of Its Thermal Stability. Angew.Chem.Int.Ed.Engl., 59:343-351, 2020 Cited by PubMed Abstract: 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. PubMed: 31778296DOI: 10.1002/anie.201911554 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.3 Å) |
Structure validation
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