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Synergism Between Halide Binding and Proton Transport in a CLC-type Exchanger

Accardi, Alessio, Lobet, Séverine, Williams, Carole, Miller, Christopher, Dutzler, Raimund·2006·Journal of Molecular Biology
DOI 10.1016/j.jmb.2006.07.081
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Abstract

The Cl-/H+ exchange-transporter CLC-ec1 mediates stoichiometric transmembrane exchange of two Cl- ions for one proton. A conserved tyrosine residue, Y445, coordinates one of the bound Cl- ions visible in the structure of this protein and is located near the intersection of the Cl- and H+ pathways. Mutants of this tyrosine were scrutinized for effects on the coupled transport of Cl- and H+ determined electrophysiologically and on protein structure determined crystallographically. Despite the strong conservation of Y445 in the CLC family, substitution of F or W at this position preserves wild-type transport behavior. Substitution by A, E, or H, however, produces uncoupled proteins with robust Cl- transport but greatly impaired movement of H+. The obligatory 2 Cl-/1 H+ stoichiometry is thus lost in these mutants. The structures of all the mutants are essentially identical to wild-type, but apparent anion occupancy in the Cl- binding region correlates with functional H+ coupling. In particular, as determined by anomalous diffraction in crystals grown in Br-, an electrophysiologically competent Cl- analogue, the well-coupled transporters show strong Br- electron density at the "inner" and "central" Cl- binding sites. However, in the uncoupled mutants, Br- density is absent at the central site, while still present at the inner site. An additional mutant, Y445L, is intermediate in both functional and structural features. This mutant clearly exchanges H+ for Cl-, but at a reduced H+-…

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Research works printed but not linked: 32

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Metadata

Authors
Accardi, A., Lobet, S., Williams, C., Miller, C., & Dutzler, R.
Venue
Journal of Molecular Biology
Publisher
Elsevier BV
Published
2006-09
Volume
362
Issue
4
Pages
691-699
ISSN
0022-2836
DOI
10.1016/j.jmb.2006.07.081
Cited by
106
References
0
Language
en
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