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J. Biol. Chem., Vol. 276, Issue 48, 44993-45000, November 30, 2001
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From the 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-Å 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.
The atomic coordinates and the structure factors (code 1K0M, 1K0N, and 1K0O) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).
Crystal Structure of a Soluble Form of the Intracellular Chloride
Ion Channel CLIC1 (NCC27) at 1.4-Å Resolution*
§,§¶,
,,,,,,,,,,,, and§¶¶
Initiative for Biomolecular Structure,
School of Physics and the §§ Department of
Medicine, University of New South Wales, New South Wales 2052, Australia, the Centre for Immunology, St. Vincent's Hospital
and University of New South Wales, Sydney New South Wales 2010, Australia, and the ** Dipartimento di Biologia Cellulare e
dello Sviluppo and the Dipartimento di
Fisiologia Umana e Farmacologia, Universita "La Sapienza," 00185 Roma, Italy
*
This work was supported by grants from the National Health
and Medical Research Council of Australia and by the University of New
South Wales Capital Grants scheme; Australian Research Council Research
Infrastructure Equipment and Facilities Program grants; St. Vincent's
Hospital, Sydney; Meriton Apartments Pty Ltd through a research and
development syndicate arranged by Macquarie Bank Limited; New
South Wales Health Research and Development infrastructure grant; and
the Rebecca L. Cooper Medical Research Foundation. This work was also
funded by grants from the Ministero dell'Universitá e della
Ricerca Scientifica e Tecnologica (Italian Minister) and Consiglio
Nazionale delle Ricerche (National Research Center) (to M. M.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
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