5NDC
Structure of ba3-type cytochrome c oxidase from Thermus thermophilus by serial femtosecond crystallography
Summary for 5NDC
| Entry DOI | 10.2210/pdb5ndc/pdb |
| Descriptor | Cytochrome c oxidase subunit 1, Cytochrome c oxidase subunit 2, Cytochrome c oxidase polypeptide IIA, ... (9 entities in total) |
| Functional Keywords | cytochrome c oxidase, oxidoreductase, sfx, respiratory chain enzyme |
| Biological source | Thermus thermophilus More |
| Total number of polymer chains | 3 |
| Total formula weight | 92967.22 |
| Authors | Andersson, R.,Safari, C.,Dods, R.,Nango, E.,Tanaka, R.,Nakane, T.,Tono, K.,Joti, Y.,Bath, P.,Dunevall, E.,Bosman, E.,Nureki, O.,Iwata, S.,Neutze, R.,Branden, G. (deposition date: 2017-03-08, release date: 2017-08-23, Last modification date: 2024-01-17) |
| Primary citation | Andersson, R.,Safari, C.,Dods, R.,Nango, E.,Tanaka, R.,Yamashita, A.,Nakane, T.,Tono, K.,Joti, Y.,Bath, P.,Dunevall, E.,Bosman, R.,Nureki, O.,Iwata, S.,Neutze, R.,Branden, G. Serial femtosecond crystallography structure of cytochrome c oxidase at room temperature. Sci Rep, 7:4518-4518, 2017 Cited by PubMed Abstract: Cytochrome c oxidase catalyses the reduction of molecular oxygen to water while the energy released in this process is used to pump protons across a biological membrane. Although an extremely well-studied biological system, the molecular mechanism of proton pumping by cytochrome c oxidase is still not understood. Here we report a method to produce large quantities of highly diffracting microcrystals of ba -type cytochrome c oxidase from Thermus thermophilus suitable for serial femtosecond crystallography. The room-temperature structure of cytochrome c oxidase is solved to 2.3 Å resolution from data collected at an X-ray Free Electron Laser. We find overall agreement with earlier X-ray structures solved from diffraction data collected at cryogenic temperature. Previous structures solved from synchrotron radiation data, however, have shown conflicting results regarding the identity of the active-site ligand. Our room-temperature structure, which is free from the effects of radiation damage, reveals that a single-oxygen species in the form of a water molecule or hydroxide ion is bound in the active site. Structural differences between the ba -type and aa -type cytochrome c oxidases around the proton-loading site are also described. PubMed: 28674417DOI: 10.1038/s41598-017-04817-z PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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