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ID 48606
file
creator
Oki, Hiroya
Kawahara, Kazuki
Yamane, Daisuke
Yamanaka, Masaru
Maruno, Takahiro
Kobayashi, Yuji
Masanari, Misa
Wakai, Satoshi
Nishihara, Hirofumi
Ohkubo, Tadayasu
subject
protein stability
cytochrome c
thermophile
protein structure
mutagenesis
ligand-binding
abstract
Thermophilic Hydrogenophilus thermoluteolus cytochrome c0 (PHCP) exhibits higher thermal stability than a mesophilic counterpart, Allochromatium vinosum cytochrome c0 (AVCP), which has a homo-dimeric structure and ligand-binding ability. To understand the thermal stability mechanism and ligand-binding ability of the thermally stable PHCP protein, the crystal structure of PHCP was first determined. It formed a homo-dimeric structure, the main chain root mean square deviation (rmsd) value between PHCP and AVCP being 0.65 A ° . In the PHCP structure, six specific residues appeared to strengthen the heme-related and subunit–subunit interactions, which were not conserved in the AVCP structure. PHCP variants having altered subunit–subunit interactions were more severely destabilized than ones having altered heme-related interactions. The PHCP structure further revealed a ligand-binding channel and a penta-coordinated heme, as observed in the AVCP protein. A spectroscopic study clearly showed that some ligands were bound to the PHCP protein. It is concluded that the dimeric PHCP from the thermophile is effectively stabilized through heme-related and subunit–subunit interactions with conservation of the ligand-binding ability.
description
This work was performed under the Cooperative Research Program of the “Network Joint Research Center for Materials and Devices”.
journal title
Protein Science
volume
Volume 26
issue
Issue 4
start page
737
end page
748
date of issued
2017-03-06
publisher
Wiley
issn
0961-8368
1469-896X
publisher doi
pubmed id
language
eng
nii type
Journal Article
HU type
Journal Articles
DCMI type
text
format
application/pdf
text version
publisher
rights
© 2017 The Authors Protein Science published by Wiley Periodicals, Inc. on behalf of The Protein Society. This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
relation url
department
Graduate School of Biosphere Science