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TitleHow Does a Microbial Rhodopsin RxR Realize Its Exceptionally High Thermostability with the Proton-Pumping Function Being Retained?
Journal, issue, pagesJ. Phys. Chem. B, Vol. 124, Page 990-1000, Year 2020
Publish dateJul 8, 2019 (structure data deposition date)
AuthorsHayashi, T. / Yasuda, S. / Suzuki, K. / Akiyama, T. / Kanehara, K. / Kojima, K. / Tanabe, M. / Kato, R. / Senda, T. / Sudo, Y. ...Hayashi, T. / Yasuda, S. / Suzuki, K. / Akiyama, T. / Kanehara, K. / Kojima, K. / Tanabe, M. / Kato, R. / Senda, T. / Sudo, Y. / Murata, T. / Kinoshita, M.
External linksJ. Phys. Chem. B / PubMed:31955569
MethodsX-ray diffraction
Resolution1.84 Å
Structure data

PDB-6kfq:
Crystal structure of thermophilic rhodopsin from Rubrobacter xylanophilus
Method: X-RAY DIFFRACTION / Resolution: 1.84 Å

Chemicals

ChemComp-MPG:
[(Z)-octadec-9-enyl] (2R)-2,3-bis(oxidanyl)propanoate

ChemComp-RET:
RETINAL

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

Source
  • rubrobacter xylanophilus (strain dsm 9941 / nbrc 16129) (bacteria)
KeywordsTRANSPORT PROTEIN / Rhodopsin / Transporter / H+ transport

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