5B6Q

Crystal structure of monomeric cytochrome c5 from Shewanella violacea

Summary for 5B6Q

• Entry DOI: 10.2210/pdb5b6q/pdb
• Descriptor: Soluble cytochrome cA, HEME C, IMIDAZOLE, ... (4 entities in total)
• Functional Keywords: cytochrome c5, protein stability, shewanella, electron transport
• Biological source: Shewanella violacea
• Total number of polymer chains: 2
• Total formula weight: 17332.30

Authors

Masanari, M.,Fujii, S.,Kawahara, K.,Oki, H.,Tsujino, H.,Maruno, T.,Kobayashi, Y.,Ohkubo, T.,Nishiyama, M.,Harada, Y.,Wakai, S.,Sambongi, Y. (deposition date: 2016-06-01, release date: 2016-10-19, Last modification date: 2024-11-13)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.78 Å)