ArticleBiochemistry2011
Structure of a slow CLC Cl⁻/H+ antiporter from a cyanobacterium.
Article in Biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 25 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
25 citing papers in PubMed, 36 citations in OpenAlex.
- Molecular simulations meet personalized medicine: The mechanism of action of CLC-5 antiporter and the origin of Dent's disease.PNAS nexus · 2025Article
- Divergent CleLife · 2020Article
- Mutation of external glutamate residue reveals a new intermediate transport state and anion binding site in a CLC ClProceedings of the National Academy of Sciences of the United States of America · 2019Article
- Structure of the CLC-1 chloride channel fromeLife · 2018Article
- Two Cl Ions and a Glu Compete for a Helix Cage in the CLC Proton/ClBiophysical journal · 2017Article
- Article
- Molecular Basis for Differential Anion Binding and Proton Coupling in the Cl(-)/H(+) Exchanger ClC-ec1.Journal of the American Chemical Society · 2016Article
- Revealing an outward-facing open conformational state in a CLC Cl(-)/H(+) exchange transporter.eLife · 2016Article
- A tale of two CLCs: biophysical insights toward understanding ClC-5 and ClC-7 function in endosomes and lysosomes.The Journal of physiology · 2015Review
- Structure and gating of CLC channels and exchangers.The Journal of physiology · 2015Review
- In the beginning: a personal reminiscence on the origin and legacy of ClC-0, the 'Torpedo Cl(-) channel'.The Journal of physiology · 2015Review
- A Proteoliposome-Based Efflux Assay to Determine Single-molecule Properties of Cl- Channels and Transporters.Journal of visualized experiments : JoVE · 2015Article
- 13C NMR detects conformational change in the 100-kD membrane transporter ClC-ec1.Journal of biomolecular NMR · 2015Article
- ClC-1 chloride channels: state-of-the-art research and future challenges.Frontiers in cellular neuroscience · 2015Review
- Salt acclimation of cyanobacteria and their application in biotechnology.Life (Basel, Switzerland) · 2014Review
- Electrostatic interactions and hydrogen bond dynamics in chloride pumping by halorhodopsin.Biochimica et biophysica acta · 2014Article
- Conformational changes required for H(+)/Cl(-) exchange mediated by a CLC transporter.Nature structural & molecular biology · 2014Article
- Prerequisites to proton transport in the bacterial ClC-ec1 Cl-/H+ exchanger.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- CLC channel function and dysfunction in health and disease.Frontiers in physiology · 2014Review
- Fluoride-dependent interruption of the transport cycle of a CLC Cl-/H+ antiporter.Nature chemical biology · 2013Article
Corrections and comments
- Erratum issued
Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
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 represents a functional outlier. Here, we characterize a CLC Cl(-)/H(+) antiporter from the cyanobacterium Synechocystis sp. PCC6803 (SY) and determine its crystal structure at 3.2 Å resolution. The structure of SY is nearly identical to that of EC, with all residues involved in Cl(-) binding and proton coupling structurally similar to their equivalents in EC. SY actively pumps protons into liposomes against a gradient and moves Cl(-) at ∼20 s(-1), 1% of the EC rate. Electrostatic calculations, used to identify residues contributing to ion binding energetics in SY and EC, highlight two residues flanking the external binding site that are destabilizing for Cl(-) binding in SY and stabilizing in EC. Mutation of these two residues in SY to their counterparts in EC accelerates transport to ∼150 s(-1), allowing measurement of Cl(-)/H(+) stoichiometry of 2/1. SY thus shares a similar structure and a common transport mechanism to EC, but it is by comparison slow, a result that refutes the idea that the transport mechanism of CLCs leads to intrinsically high rates.
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Registered trials
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