Structural characteristics of the redox-sensing coiled coil in the voltage-gated H^+ channel

Fujiwara, Yuichoiro; Takeshita, Kohei; Nakagawa, Atushi et al.

Journal of Biological Chemistry, 2013, 288(25), 17968-17975

Number of Access:663（2025-07-18 09:54 Counts）

Identifier to cite or link to this item: https://hdl.handle.net/11094/73662

Link to primary information 

File Format Terms of use Size Views Date.Available Description information
JBC288_25_17968 pdf None 1.82 MB 181 2019.12.06  

Item Information

Output File Export EndNote Basic Export Mendeley

Title
Structural characteristics of the redox-sensing coiled coil in the voltage-gated H^+ channel
Creator
CreatorName
Fujiwara, Yuichoiro
NRID
1000080346808 1000080346808
CreatorName
Takeshita, Kohei
NRID
1000020188890 1000020188890
ORCID
0000-0002-1700-7861 0000-0002-1700-7861
researchmap permalink
atsushi_nakagawa atsushi_nakagawa
Scopus Author ID
7202934909 7202934909
CreatorName
Nakagawa, Atushi
NRID
1000080201987 1000080201987
researchmap permalink
yasushiokamura yasushiokamura
Scopus Author ID
55322083200 55322083200
ORCID
0000-0001-5386-7968 0000-0001-5386-7968
CreatorName
Okamura, Yasushi
Description
This research was originally published in Journal of Biological Chemistry. Yuichiro Fujiwara, Kohei Takeshita, Atsushi Nakagawa and Yasushi Okamura. Structural characteristics of the redox-sensing coiled coil in the voltage-gated H^+ channel. Journal of Biological Chemistry. 2013; 288, 17968-17975. © the American Society for Biochemistry and Molecular Biology.
Abstract
Oxidation is an important biochemical defense mechanism, but it also elicits toxicity; therefore, oxidation must be under strict control. In phagocytotic events in neutrophils, the voltagegated H^＋ (Hv) channel is a key regulator of the production of reactive oxygen species against invading bacteria. The cytoplasmic domain of the Hv channel forms a dimeric coiled coil underpinning a dimerized functional unit. Importantly, in the alignment of the coiled-coil core, a conserved cysteine residue forms a potential intersubunit disulfide bond. In this study, we solved the crystal structures of the coiled-coil domain in reduced, oxidized, and mutated (Cys → Ser) states. The crystal structures indicate that a pair of Cys residues forms an intersubunit disulfide bond dependent on the redox conditions. CD spectroscopy revealed that the disulfide bond increases the thermal stability of the coiled-coil protein. We also reveal that two thiol modifier molecules are able to bind to Cys in a redox-dependent manner without disruption of the dimeric coiled-coil assembly. Thus, the biochemical properties of the cytoplasmic coiled-coil domain in the Hv channel depend on the redox condition, which may play a role in redox sensing in the phagosome.
Publisher
American Society for Biochemistry and Molecular Biology
Source Title
Journal of Biological Chemistry
Volume (Issue)
288(25)
Page
17968-17975
Date of Issued
2013-06
Language
English
Handle URL
https://hdl.handle.net/11094/73662
eISSN
1083351X
NCID
AA1202441X
Relation.isIdenticalTo
DOI (Publisher Version)
https://doi.org/10.1074/jbc.M113.459024
PMID
23667254
Access Rights
open access
CopyRight
© the American Society for Biochemistry and Molecular Biology.
oaire:version
Version of Record
Category
学術雑誌論文 Journal Article