7YRA
Crystal structure of [2Fe-2S]-TtPetA
Summary for 7YRA
| Entry DOI | 10.2210/pdb7yra/pdb |
| Related | 7YR9 |
| Descriptor | Ubiquinol-cytochrome c reductase iron-sulfur subunit, FE2/S2 (INORGANIC) CLUSTER, SULFATE ION, ... (6 entities in total) |
| Functional Keywords | rieske, iron-sulfur cluster, metal binding, electron transport |
| Biological source | Thermochromatium tepidum |
| Total number of polymer chains | 2 |
| Total formula weight | 33947.40 |
| Authors | Tsutsumi, E.,Niwa, S.,Takeda, K. (deposition date: 2022-08-09, release date: 2023-09-20, Last modification date: 2024-10-23) |
| Primary citation | Tsutsumi, E.,Niwa, S.,Takeda, R.,Sakamoto, N.,Okatsu, K.,Fukai, S.,Ago, H.,Nagao, S.,Sekiguchi, H.,Takeda, K. Structure of a putative immature form of a Rieske-type iron-sulfur protein in complex with zinc chloride. Commun Chem, 6:190-190, 2023 Cited by PubMed Abstract: Iron-sulfur clusters are prosthetic groups of proteins involved in various biological processes. However, details of the immature state of the iron-sulfur cluster into proteins have not yet been elucidated. We report here the first structural analysis of the Zn-containing form of a Rieske-type iron-sulfur protein, PetA, from Thermochromatium tepidum (TtPetA) by X-ray crystallography and small-angle X-ray scattering analysis. The Zn-containing form of TtPetA was indicated to be a dimer in solution. The zinc ion adopts a regular tetra-coordination with two chloride ions and two cysteine residues. Only a histidine residue in the cluster-binding site exhibited a conformational difference from the [2Fe-2S] containing form. The Zn-containing structure indicates that the conformation of the cluster binding site is already constructed and stabilized before insertion of [2Fe-2S]. The binding mode of ZnCl, similar to the [2Fe-2S] cluster, suggests that the zinc ions might be involved in the insertion of the [2Fe-2S] cluster. PubMed: 37689761DOI: 10.1038/s42004-023-01000-6 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.79 Å) |
Structure validation
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