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5G54

The crystal structure of light-driven chloride pump ClR at pH 4.5

Summary for 5G54
Entry DOI10.2210/pdb5g54/pdb
DescriptorChloride pumping rhodopsin, CHLORIDE ION, OLEIC ACID, ... (5 entities in total)
Functional Keywordssignaling protein, proetin
Biological sourceNonlabens marinus S1-08
Total number of polymer chains1
Total formula weight33104.79
Authors
Kim, K.L.,Kwon, S.K.,Jun, S.H.,Cha, J.S.,Kim, H.Y.,Kim, J.H.,Cho, H.S. (deposition date: 2016-05-19, release date: 2016-10-19, Last modification date: 2024-10-23)
Primary citationKim, K.,Kwon, S.,Jun, S.,Cha, J.S.,Kim, H.,Lee, W.,Kim, J.F.,Cho, H.
Crystal Structure and Functional Characterization of a Light-Driven Chloride Pump Having an Ntq Motif.
Nat.Commun., 7:12677-, 2016
Cited by
PubMed Abstract: A novel light-driven chloride-pumping rhodopsin (ClR) containing an 'NTQ motif' in its putative ion conduction pathway has been discovered and functionally characterized in a genomic analysis study of a marine bacterium. Here we report the crystal structure of ClR from the flavobacterium Nonlabens marinus S1-08(T) determined under two conditions at 2.0 and 1.56 Å resolutions. The structures reveal two chloride-binding sites, one around the protonated Schiff base and the other on a cytoplasmic loop. We identify a '3 omega motif' formed by three non-consecutive aromatic amino acids that is correlated with the B-C loop orientation. Detailed ClR structural analyses with functional studies in E. coli reveal the chloride ion transduction pathway. Our results help understand the molecular mechanism and physiological role of ClR and provide a structural basis for optogenetic applications.
PubMed: 27554809
DOI: 10.1038/NCOMMS12677
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2 Å)
Structure validation

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