5B6Q

Crystal structure of monomeric cytochrome c5 from Shewanella violacea

5B6Q の概要

• エントリーDOI: 10.2210/pdb5b6q/pdb
• 分子名称: Soluble cytochrome cA, HEME C, IMIDAZOLE, ... (4 entities in total)
• 機能のキーワード: cytochrome c5, protein stability, shewanella, electron transport
• 由来する生物種: Shewanella violacea
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 17332.30

構造登録者

Masanari, M.,Fujii, S.,Kawahara, K.,Oki, H.,Tsujino, H.,Maruno, T.,Kobayashi, Y.,Ohkubo, T.,Nishiyama, M.,Harada, Y.,Wakai, S.,Sambongi, Y. (登録日: 2016-06-01, 公開日: 2016-10-19, 最終更新日: 2024-11-13)

主引用文献

Masanari, M.,Fujii, S.,Kawahara, K.,Oki, H.,Tsujino, H.,Maruno, T.,Kobayashi, Y.,Ohkubo, T.,Wakai, S.,Sambongi, Y.
Comparative study on stabilization mechanism of monomeric cytochrome c5 from deep-sea piezophilic Shewanella violacea
Biosci.Biotechnol.Biochem., 2016

PubMed Abstract: Monomeric cytochrome c from deep-sea piezophilic Shewanella violacea (SVcytc) was stable against heat and denaturant compared with the homologous protein from shallow-sea piezo-sensitive Shewanella livingstonensis (SLcytc). Here, the SVcytc crystal 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 SLcytc, 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 SVcytc was isolated from a deep-sea piezophilic bacterium, the present comparative study indicates that adaptation of monomeric SVcytc to high pressure environments results in stabilization against heat.

PubMed: 27648635
DOI: 10.1080/09168451.2016.1232155

実験手法

X-RAY DIFFRACTION (1.78 Å)