Salt bridge in the conserved His-Asp cluster in Gloeobacter rhodopsin contributes to trimer formation

Tsukamoto, Takashi; Kikukawa, Takashi; Kurata, Takuro et al.

FEBS Letters, 2013, 587(4), 322-327

Permalink : https://hdl.handle.net/2115/52199

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アクセス権
open access
URI
https://hdl.handle.net/2115/52199
タイトル
Salt bridge in the conserved His-Asp cluster in Gloeobacter rhodopsin contributes to trimer formation
著者
Tsukamoto, Takashi ; Kikukawa, Takashi ; Kurata, Takuro ; Jung, Kwang-Hwan ; Kamo, Naoki ; Demura, Makoto
著者名
Tsukamoto, Takashi
e-Rad_Researcher
20281842
著者名
Kikukawa, Takashi
著者名
Kurata, Takuro
著者名
Jung, Kwang-Hwan
著者名
Kamo, Naoki
e-Rad_Researcher
70188704
著者名
Demura, Makoto
言語
英語
キーワード
Microbial rhodopsin
Histidine-Aspartate cluster
Quaternary structure
Protonation
Size-exclusion chromatography
Circular dichroism spectroscopy
発行日
2013-02-14
出版者
Elsevier B.V.
収録物名
FEBS Letters
巻(号)
587(4)
ページ
322-327
抄録
Gloeobacter rhodopsin (GR) is a eubacterial proton pump having a highly conserved histidine near the retinal Schiff base counter-ion, aspartate. Various interactions between His and Asp of the eubacterial proton pump have been reported. Here, we showed the pH-dependent trimer/monomer transition of GR in the presence of dodecyl-β-D-maltoside by size-exclusion chromatography. The pH dependence was closely related to the protonation state of the counter-ion, Asp121. For the H87M mutant, pH dependence disappeared and a monomer became dominant. We concluded that the formation or breaking of the salt bridge between His87 and Asp121 inside the protein changes the quaternary structure.
資源タイプ
学術雑誌論文
出版タイプ
Accepted Manuscript
PISSN
0014-5793
関連情報
PMID
23313943
関連情報 (isVersionOf)
出版社版DOI
https://doi.org/10.1016/j.febslet.2012.12.022