ArticleBiophysical journal2004
Anion pathway and potential energy profiles along curvilinear bacterial ClC Cl- pores: electrostatic effects of charged residues.
Article in Biophysical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 64 citations in OpenAlex.
- Electrostatic Potential of Functional Cations as a Predictor of Hydroxide Diffusion Pathways in Nanoconfined Environments of Anion Exchange Membranes.The journal of physical chemistry letters · 2024Article
- Multiscale Kinetic Modeling Reveals an Ensemble of ClJournal of the American Chemical Society · 2018Article
- Chloride Ion Transport by theFrontiers in chemistry · 2018Article
- Gating the glutamate gate of CLC-2 chloride channel by pore occupancy.The Journal of general physiology · 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
- Influences of mutations on the electrostatic binding free energies of chloride ions in Escherichia coli ClC.The journal of physical chemistry. B · 2012Article
- Solvation free energies of glutamate and its metal complexes: a computer simulation study.Journal of molecular modeling · 2011Article
- A three-state multi-ion kinetic model for conduction properties of ClC-0 chloride channel.Biophysical journal · 2010Article
- Electroelastic coupling between membrane surface fluctuations and membrane-embedded charges: continuum multidielectric treatment.The Journal of chemical physics · 2010Article
- Secondary water pore formation for proton transport in a ClC exchanger revealed by an atomistic molecular-dynamics simulation.Biophysical journal · 2010Article
- Shape-Dependent Global Deformation Modes of Large Protein Structures.Journal of molecular structure · 2010Article
- Antiport mechanism for Cl(-)/H(+) in ClC-ec1 from normal-mode analysis.Biophysical journal · 2010Article
- Proton transport pathway in the ClC Cl-/H+ antiporter.Biophysical journal · 2009Article
- Voltage-dependent and -independent titration of specific residues accounts for complex gating of a ClC chloride channel by extracellular protons.The Journal of physiology · 2009Article
- Conformational changes in the selectivity filter of the open-state KcsA channel: an energy minimization study.Biophysical journal · 2008Article
- The role of a conserved lysine in chloride- and voltage-dependent ClC-0 fast gating.The Journal of general physiology · 2007Article
- Roles of K149, G352, and H401 in the channel functions of ClC-0: testing the predictions from theoretical calculations.The Journal of general physiology · 2006Article
- Electrostatics in the cytoplasmic pore produce intrinsic inward rectification in kir2.1 channels.The Journal of general physiology · 2005Article
- Cysteine accessibility in ClC-0 supports conservation of the ClC intracellular vestibule.The Journal of general physiology · 2005Article
- Water and ion permeation in bAQP1 and GlpF channels: a kinetic Monte Carlo study.Biophysical journal · 2004Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
X-ray structures permit theoretical study of Cl(-) permeation along bacterial ClC Cl(-) pores. We determined the lowest energy curvilinear pathway, identified anion-coordinating amino acids, and calculated the electrostatic potential energy profiles. We find that all four bacterial ClC Cl(-) crystal structures correspond to closed states. E148 and S107 side chains form steric barriers on both sides of the crystal binding site in the StClC wild-type and EcClC wild-type crystals; both the EcClC(E148A) and EcClC(E148Q) mutants are blocked at the S107 site. We studied the effect that mutating the charge of some strongly conserved pore-lining amino acids has on the electrostatic potential energy profiles. When E148 is neutralized, it creates an electrostatic trap, binding the ion near midmembrane. This suggests a possible electrostatic mechanism for controlling anion flow: neutralize E148, displace the side chain of E148 from the pore pathway to relieve the steric barrier, then trap the anion at midmembrane, and finally either deprotonate E148 and block the pore (pore closure) or bring a second Cl(-) into the pore to promote anion flow (pore conductance). Side-chain displacement may arise by competition for the binding site between the oxygens of E148 and the anion moving down the electrostatic energy gradient. We also find that the charge state of E111 and E113 may electrostatically control anion conductance and occupancy of the binding site within the cytoplasmic pore.
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