1K0O

Crystal structure of a soluble form of CLIC1. An intracellular chloride ion channel

Summary for 1K0O

• Entry DOI: 10.2210/pdb1k0o/pdb
• Descriptor: CHLORIDE INTRACELLULAR CHANNEL PROTEIN 1 (2 entities in total)
• Functional Keywords: glutathione-s-transferase superfamily, clic1, ncc27, chloride ion channel, metal transport
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus: O00299
• Total number of polymer chains: 2
• Total formula weight: 53763.21

Authors

Harrop, S.J.,DeMaere, M.Z.,Fairlie, W.D.,Reztsova, T.,Valenzuela, S.M.,Mazzanti, M.,Tonini, R.,Qiu, M.R.,Jankova, L.,Warton, K.,Bauskin, A.R.,Wu, W.M.,Pankhurst, S.,Campbell, T.J.,Breit, S.N.,Curmi, P.M.G. (deposition date: 2001-09-19, release date: 2001-12-12, Last modification date: 2024-02-07)

Primary citation

Harrop, S.J.,DeMaere, M.Z.,Fairlie, W.D.,Reztsova, T.,Valenzuela, S.M.,Mazzanti, M.,Tonini, R.,Qiu, M.R.,Jankova, L.,Warton, K.,Bauskin, A.R.,Wu, W.M.,Pankhurst, S.,Campbell, T.J.,Breit, S.N.,Curmi, P.M.
Crystal structure of a soluble form of the intracellular chloride ion channel CLIC1 (NCC27) at 1.4-A resolution.
J.Biol.Chem., 276:44993-45000, 2001

PubMed Abstract: CLIC1 (NCC27) is a member of the highly conserved class of chloride ion channels that exists in both soluble and integral membrane forms. Purified CLIC1 can integrate into synthetic lipid bilayers forming a chloride channel with similar properties to those observed in vivo. The structure of the soluble form of CLIC1 has been determined at 1.4-A resolution. The protein is monomeric and structurally homologous to the glutathione S-transferase superfamily, and it has a redox-active site resembling glutaredoxin. The structure of the complex of CLIC1 with glutathione shows that glutathione occupies the redox-active site, which is adjacent to an open, elongated slot lined by basic residues. Integration of CLIC1 into the membrane is likely to require a major structural rearrangement, probably of the N-domain (residues 1-90), with the putative transmembrane helix arising from residues in the vicinity of the redox-active site. The structure indicates that CLIC1 is likely to be controlled by redox-dependent processes.

PubMed: 11551966
DOI: 10.1074/jbc.M107804200

Experimental method

X-RAY DIFFRACTION (1.75 Å)