5G2C
The crystal structure of light-driven chloride pump ClR (T102D) mutant at pH 4.5.
Summary for 5G2C
Entry DOI | 10.2210/pdb5g2c/pdb |
Related | 5G28 5G29 5G2A 5G2D |
Descriptor | CHLORIDE PUMPING RHODOPSIN, OLEIC ACID, CHLORIDE ION, ... (6 entities in total) |
Functional Keywords | transport protein |
Biological source | NONLABENS MARINUS S1-08 |
Total number of polymer chains | 1 |
Total formula weight | 33189.44 |
Authors | |
Primary citation | Kim, 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: 27554809DOI: 10.1038/NCOMMS12677 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.31 Å) |
Structure validation
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