7EAD

Crystal structure of beta-sheet cytochrome c prime from Thermus thermophilus.

7EAD の概要

• エントリーDOI: 10.2210/pdb7ead/pdb
• 分子名称: Cytochrome_P460 domain-containing protein, HEME C (3 entities in total)
• 機能のキーワード: cytochrome c, thermophile, electron transport
• 由来する生物種: Thermus thermophilus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15560.63

構造登録者

Yoshimi, T.,Fujii, S.,Oki, H.,Igawa, T.,Adams, R.H.,Ueda, K.,Kawahara, K.,Ohkubo, T.,Hough, A.M.,Sambongi, Y. (登録日: 2021-03-07, 公開日: 2022-03-09, 最終更新日: 2024-11-06)

主引用文献

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

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: 35647678
DOI: 10.1107/S2053230X22005088

実験手法

X-RAY DIFFRACTION (1.74 Å)