7EAD
Crystal structure of beta-sheet cytochrome c prime from Thermus thermophilus.
Summary for 7EAD
| Entry DOI | 10.2210/pdb7ead/pdb |
| Descriptor | Cytochrome_P460 domain-containing protein, HEME C (3 entities in total) |
| Functional Keywords | cytochrome c, thermophile, electron transport |
| Biological source | Thermus thermophilus |
| Total number of polymer chains | 1 |
| Total formula weight | 15560.63 |
| Authors | Yoshimi, T.,Fujii, S.,Oki, H.,Igawa, T.,Adams, R.H.,Ueda, K.,Kawahara, K.,Ohkubo, T.,Hough, A.M.,Sambongi, Y. (deposition date: 2021-03-07, release date: 2022-03-09, Last modification date: 2024-11-06) |
| Primary citation | Yoshimi, T.,Fujii, S.,Oki, H.,Igawa, T.,Adams, H.R.,Ueda, K.,Kawahara, K.,Ohkubo, T.,Hough, M.A.,Sambongi, Y. Crystal structure of thermally stable homodimeric cytochrome c'-beta from Thermus thermophilus. Acta Crystallogr.,Sect.F, 78:217-225, 2022 Cited by PubMed Abstract: Cytochrome c'-β is a heme protein that belongs to the cytochrome P460 family and consists of homodimeric subunits with a predominantly antiparallel β-sheet fold. Here, the crystal structure of cytochrome c'-β from the thermophilic Thermus thermophilus (TTCP-β) is reported at 1.74 Å resolution. TTCP-β has a typical antiparallel β-sheet fold similar to that of cytochrome c'-β from the moderately thermophilic Methylococcus capsulatus (MCCP-β). The phenylalanine cap structure around the distal side of the heme is also similar in TTCP-β and MCCP-β, indicating that both proteins similarly bind nitric oxide and carbon monoxide, as observed spectroscopically. Notably, TTCP-β exhibits a denaturation temperature of 117°C, which is higher than that of MCCP-β. Mutational analysis reveals that the increased homodimeric interface area of TTCP-β contributes to its high thermal stability. Furthermore, 14 proline residues, which are mostly located in the TTCP-β loop regions, possibly contribute to the rigid loop structure compared with MCCP-β, which has only six proline residues. These findings, together with those from phylogenetic analysis, suggest that the structures of Thermus cytochromes c'-β, including TTCP-β, are optimized for function under the high-temperature conditions in which the source organisms live. PubMed: 35647678DOI: 10.1107/S2053230X22005088 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.74 Å) |
Structure validation
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