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- Title
Comparative study on stabilization mechanism of monomeric cytochrome c 5 from deep-sea piezophilic Shewanella violacea.
- Authors
Masanari, Misa; Fujii, Sotaro; Kawahara, Kazuki; Oki, Hiroya; Tsujino, Hirofumi; Maruno, Takahiro; Kobayashi, Yuji; Ohkubo, Tadayasu; Wakai, Satoshi; Sambongi, Yoshihiro
- Abstract
Monomeric cytochromec5from deep-sea piezophilicShewanella violacea(SVcytc5) was stable against heat and denaturant compared with the homologous protein from shallow-sea piezo-sensitiveShewanella livingstonensis(SLcytc5). Here, the SVcytc5crystal structure revealed that the Lys-50 side chain on the flexible loop formed a hydrogen bond with heme whereas that of corresponding hydrophobic Leu-50 could not form such a bond in SLcytc5, which appeared to be one of possible factors responsible for the difference in stability between the two proteins. This structural insight was confirmed by a reciprocal mutagenesis study on the thermal stability of these two proteins. As SVcytc5was isolated from a deep-sea piezophilic bacterium, the present comparative study indicates that adaptation of monomeric SVcytc5to high pressure environments results in stabilization against heat. Structure ofShewanella violaceacy to chromec5revealed that Lys-50 on a flexible loop was responsible for its stability.
- Subjects
CYTOCHROME c; SHEWANELLA; CRYSTAL structure; DEEP-sea ecology; BAROPHILIC bacteria
- Publication
Bioscience, Biotechnology & Biochemistry, 2016, Vol 80, Issue 12, p2365
- ISSN
0916-8451
- Publication type
Article
- DOI
10.1080/09168451.2016.1232155