PDBsum entry 5g2c

Transport protein

PDB id

5g2c

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Contents

			Protein chain

					268 a.a.

			Ligands

					OLA ×8


					RET


					PEG

			Metals

					_CL

			Waters ×15

PDB id:

5g2c

Links

Name:

Transport protein

Title:

The crystal structure of light-driven chloride pump clr (t102d) mutant at ph 4.5.

Structure:

Chloride pumping rhodopsin. Chain: a. Fragment: seven trans-membrane. Synonym: chloride pump rhodopsin. Engineered: yes. Mutation: yes

Source:

Nonlabens marinus s1-08. Organism_taxid: 1454201. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

2.31Å

R-factor:

0.197

R-free:

0.239

Authors:

K.L.Kim,S.K.Kwon,S.H.Jun,J.S.Cha,H.Y.Kim,J.H.Kim,H.S.Cho

Key ref:

K.Kim et al. (2016). Crystal structure and functional characterization of a light-driven chloride pump having an NTQ motif. Nat Commun, 7, 12677. PubMed id: 27554809 DOI: 10.1038/ncomms12677

Date:

07-Apr-16

Release date:

19-Oct-16

PROCHECK

	Headers

	References

Protein chain

W8VZW3 (W8VZW3_9FLAO) - Chloride pumping rhodopsin from Nonlabens marinus S1-08

Seq: Struc:					272 a.a. 268 a.a.*

Key:

PfamA domain

Secondary structure

CATH domain

* PDB and UniProt seqs differ at 1 residue position (black cross)

DOI no: 10.1038/ncomms12677	Nat Commun 7:12677 (2016)
PubMed id: 27554809

Crystal structure and functional characterization of a light-driven chloride pump having an NTQ motif.
K.Kim, S.K.Kwon, S.H.Jun, J.S.Cha, H.Kim, W.Lee, J.F.Kim, H.S.Cho.

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.