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Article

Structure of a slow CLC Cl⁻/H+ antiporter from a cyanobacterium.

Biochemistry - 8 Feb 2011

Jayaram Hariharan, Robertson Janice L, Wu Fang, Williams Carole, Miller Christopher

Abstract excerpt

X-ray crystal structures have been previously determined for three CLC-type transporter homologues, but the absolute unitary transport rate is known for only one of these. The Escherichia coli Cl(-)/H(+) antiporter (EC) moves ∼2000 Cl(-) ions/s, an exceptionally high rate among membrane-transport proteins. It is not known whether such rapid turnover is characteristic of ClCs in general or if the E. coli homologue...

Topics

Amino Acid Sequence
Antiporters
Bacterial Proteins
Chloride Channels
Chlorides
Crystallography, X-Ray
Escherichia coli
Escherichia coli Proteins
Hydrogen
Kinetics
Molecular Sequence Data

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mutation

Protein Structure, Secondary

Sequence Alignment

Synechocystis

Source

Open in PubMed Open full text

Identifiers

PMID: 21174448
DOI: 10.1021/bi1019258
PMCID: PMC3164822

Genes

CLC

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 31 Aug 2026.

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