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Salt bridge in the conserved His-Asp cluster in Gloeobacter rhodopsin contributes to trimer formation
| Title: | Salt bridge in the conserved His-Asp cluster in Gloeobacter rhodopsin contributes to trimer formation |
| Authors: | Tsukamoto, Takashi Browse this author | | Kikukawa, Takashi Browse this author →KAKEN DB | | Kurata, Takuro Browse this author | | Jung, Kwang-Hwan Browse this author | | Kamo, Naoki Browse this author | | Demura, Makoto Browse this author →KAKEN DB |
| Keywords: | Microbial rhodopsin | | Histidine-Aspartate cluster | | Quaternary structure | | Protonation | | Size-exclusion chromatography | | Circular dichroism spectroscopy |
| Issue Date: | 14-Feb-2013 |
| Publisher: | Elsevier B.V. |
| Journal Title: | FEBS Letters |
| Volume: | 587 |
| Issue: | 4 |
| Start Page: | 322 |
| End Page: | 327 |
| Publisher DOI: | 10.1016/j.febslet.2012.12.022 |
| PMID: | 23313943 |
| Abstract: | 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. |
| Type: | article (author version) |
| URI: | http://hdl.handle.net/2115/52199 |
| Appears in Collections: | 生命科学院・先端生命科学研究院 (Graduate School of Life Science / Faculty of Advanced Life Science) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)
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Submitter: 出村 誠
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