Crystal structure of oxidized cytochrome c6A from Arabidopsis thaliana

Hirotaka Chida; Takeshi Yokoyama; Fumihiro Kawai; Aiko Nakazawa; Hideharu Akazaki; Yasuhiko Takayama; Takako Hirano; Kohei Suruga; Tadashi Satoh; Seiji Yamada; Ryu Kawachi; Satoru Unzai; Toshiyuki Nishio; Sam Yong Park; Tadatake Oku

doi:10.1016/j.febslet.2006.05.067

Crystal structure of oxidized cytochrome c_6A from Arabidopsis thaliana

Hirotaka Chida, Takeshi Yokoyama, Fumihiro Kawai, Aiko Nakazawa, Hideharu Akazaki, Yasuhiko Takayama, Takako Hirano, Kohei Suruga, Tadashi Satoh, Seiji Yamada, Ryu Kawachi, Satoru Unzai, Toshiyuki Nishio, Sam Yong Park, Tadatake Oku^*

^*Corresponding author for this work

Structural Biology

Research output: Contribution to journal › Article › peer-review

14 Scopus citations

Abstract

Compared with algal and cyanobacterial cytochrome c₆, cytochrome c_6A from higher plants contains an additional loop of 12 amino acid residues. We have determined the first crystal structure of cytochrome c_6A from Arabidopsis thaliana at 1.5 Å resolution in order to help elucidate its function. The overall structure of cytochrome c_6A follows the topology of class I c-type cytochromes in which the heme prosthetic group covalently binds to Cys16 and Cys19, and the iron has octahedral coordination with His20 and Met60 as the axial ligands. Two cysteine residues (Cys67 and Cys73) within the characteristic 12 amino acids loop form a disulfide bond, contributing to the structural stability of cytochrome c_6A. Our model provides a chemical basis for the known low redox potential of cytochrome c_6A which makes it an unsuitable electron carrier between cytochrome b₆f and PSI.

Original language	English
Pages (from-to)	3763-3768
Number of pages	6
Journal	FEBS Letters
Volume	580
Issue number	15
DOIs	https://doi.org/10.1016/j.febslet.2006.05.067
State	Published - 2006/06/26

Keywords

Arabidopsis thaliana
Crystal structure
Cytochrome c
Electron transfer

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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10.1016/j.febslet.2006.05.067

Cite this

@article{e4cd8937e746456ea2dc153822b4d13c,

title = "Crystal structure of oxidized cytochrome c6A from Arabidopsis thaliana",

abstract = "Compared with algal and cyanobacterial cytochrome c6, cytochrome c6A from higher plants contains an additional loop of 12 amino acid residues. We have determined the first crystal structure of cytochrome c6A from Arabidopsis thaliana at 1.5 {\AA} resolution in order to help elucidate its function. The overall structure of cytochrome c6A follows the topology of class I c-type cytochromes in which the heme prosthetic group covalently binds to Cys16 and Cys19, and the iron has octahedral coordination with His20 and Met60 as the axial ligands. Two cysteine residues (Cys67 and Cys73) within the characteristic 12 amino acids loop form a disulfide bond, contributing to the structural stability of cytochrome c6A. Our model provides a chemical basis for the known low redox potential of cytochrome c6A which makes it an unsuitable electron carrier between cytochrome b6f and PSI.",

keywords = "Arabidopsis thaliana, Crystal structure, Cytochrome c, Electron transfer",

author = "Hirotaka Chida and Takeshi Yokoyama and Fumihiro Kawai and Aiko Nakazawa and Hideharu Akazaki and Yasuhiko Takayama and Takako Hirano and Kohei Suruga and Tadashi Satoh and Seiji Yamada and Ryu Kawachi and Satoru Unzai and Toshiyuki Nishio and Park, {Sam Yong} and Tadatake Oku",

note = "Funding Information: We are indebted to Dr. Yasuhiro Isogai of RIKEN for valuable discussions. Thanks to Messrs. Hirotaka Hasegawa and Daisuke Tamura, and Mses. Akiko Miyake, Ichie Murai and Mikiko Hasegawa of Nihon University for the purification of cytochrome c 6A . This work was supported in part by a Grant-in-Aid for the 21st Century{\textquoteright}s Center of Excellence (COE) program (Prof. Sasaki) and for Scientific Research (C) from the Ministry of Education, Culture, Sports, Science and Technology of Japan (2005).",

year = "2006",

month = jun,

day = "26",

doi = "10.1016/j.febslet.2006.05.067",

language = "英語",

volume = "580",

pages = "3763--3768",

journal = "FEBS Letters",

issn = "0014-5793",

publisher = "John Wiley and Sons Inc.",

number = "15",

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TY - JOUR

T1 - Crystal structure of oxidized cytochrome c6A from Arabidopsis thaliana

AU - Chida, Hirotaka

AU - Yokoyama, Takeshi

AU - Kawai, Fumihiro

AU - Nakazawa, Aiko

AU - Akazaki, Hideharu

AU - Takayama, Yasuhiko

AU - Hirano, Takako

AU - Suruga, Kohei

AU - Satoh, Tadashi

AU - Yamada, Seiji

AU - Kawachi, Ryu

AU - Unzai, Satoru

AU - Nishio, Toshiyuki

AU - Park, Sam Yong

AU - Oku, Tadatake

N1 - Funding Information: We are indebted to Dr. Yasuhiro Isogai of RIKEN for valuable discussions. Thanks to Messrs. Hirotaka Hasegawa and Daisuke Tamura, and Mses. Akiko Miyake, Ichie Murai and Mikiko Hasegawa of Nihon University for the purification of cytochrome c 6A . This work was supported in part by a Grant-in-Aid for the 21st Century’s Center of Excellence (COE) program (Prof. Sasaki) and for Scientific Research (C) from the Ministry of Education, Culture, Sports, Science and Technology of Japan (2005).

PY - 2006/6/26

Y1 - 2006/6/26

N2 - Compared with algal and cyanobacterial cytochrome c6, cytochrome c6A from higher plants contains an additional loop of 12 amino acid residues. We have determined the first crystal structure of cytochrome c6A from Arabidopsis thaliana at 1.5 Å resolution in order to help elucidate its function. The overall structure of cytochrome c6A follows the topology of class I c-type cytochromes in which the heme prosthetic group covalently binds to Cys16 and Cys19, and the iron has octahedral coordination with His20 and Met60 as the axial ligands. Two cysteine residues (Cys67 and Cys73) within the characteristic 12 amino acids loop form a disulfide bond, contributing to the structural stability of cytochrome c6A. Our model provides a chemical basis for the known low redox potential of cytochrome c6A which makes it an unsuitable electron carrier between cytochrome b6f and PSI.

AB - Compared with algal and cyanobacterial cytochrome c6, cytochrome c6A from higher plants contains an additional loop of 12 amino acid residues. We have determined the first crystal structure of cytochrome c6A from Arabidopsis thaliana at 1.5 Å resolution in order to help elucidate its function. The overall structure of cytochrome c6A follows the topology of class I c-type cytochromes in which the heme prosthetic group covalently binds to Cys16 and Cys19, and the iron has octahedral coordination with His20 and Met60 as the axial ligands. Two cysteine residues (Cys67 and Cys73) within the characteristic 12 amino acids loop form a disulfide bond, contributing to the structural stability of cytochrome c6A. Our model provides a chemical basis for the known low redox potential of cytochrome c6A which makes it an unsuitable electron carrier between cytochrome b6f and PSI.

KW - Arabidopsis thaliana

KW - Crystal structure

KW - Cytochrome c

KW - Electron transfer

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DO - 10.1016/j.febslet.2006.05.067

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