期刊
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
卷 78, 期 -, 页码 217-225出版社
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S2053230X22005088
关键词
crystal structure; cytochrome c '-beta; protein thermal stability; homodimeric interface; Thermus thermophilus
资金
- Ministry of Education, Culture, Sports, Science and Technology of Japan [26240045, 16K07692]
- Ministry of Education, Culture, Sports, Science and Technology in Japan [1617PD0536]
- Graduate School of Biosphere Science, Hiroshima University
- University of Essex
- Grants-in-Aid for Scientific Research [16K07692, 26240045] Funding Source: KAKEN
This study reports the crystal structure of cytochrome c'-beta from Thermus thermophilus, which exhibits high thermal stability. Mutational analysis suggests that the increased homodimeric interface area and rigid loop structure contribute to its high thermal stability.
Cytochrome c'-beta is a heme protein that belongs to the cytochrome P460 family and consists of homodimeric subunits with a predominantly antiparallel beta-sheet fold. Here, the crystal structure of cytochrome c'-beta from the thermophilic Thermus thermophilus (TTCP-beta) is reported at 1.74 angstrom resolution. TTCP-beta has a typical antiparallel beta-sheet fold similar to that of cytochrome c'-beta from the moderately thermophilic Methylococcus capsulatus (MCCP-beta). The phenylalanine cap structure around the distal side of the heme is also similar in TTCP-beta and MCCP-beta, indicating that both proteins similarly bind nitric oxide and carbon monoxide, as observed spectroscopically. Notably, TTCP-beta exhibits a denaturation temperature of 117 degrees C, which is higher than that of MCCP-beta. Mutational analysis reveals that the increased homodimeric interface area of TTCP-beta contributes to its high thermal stability. Furthermore, 14 proline residues, which are mostly located in the TTCP-beta loop regions, possibly contribute to the rigid loop structure compared with MCCP-beta, which has only six proline residues. These findings, together with those from phylogenetic analysis, suggest that the structures of Thermus cytochromes c'-beta, including TTCP-beta, are optimized for function under the high-temperature conditions in which the source organisms live.
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