Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Molecular mechanism of exchange coupling in CLC chloride/proton antiporters.
Journal, issue, pages	Nat Commun, Year 2026
Publish date	Jan 8, 2026
Authors	Deniz Aydin / Chih-Ta Chien / Jürgen Kreiter / Amy R Nava / Jasmina M Portasikova / Lukas Fojtik / Briana L Sobecks / Catalina Mosquera / Petr Man / Ron O Dror / Wah Chiu / Merritt Maduke /
PubMed Abstract	The ubiquitous CLC membrane transporters are unique in their ability to exchange anions for cations. Despite extensive study, there is no mechanistic model that fully explains their 2:1 Cl/H ...The ubiquitous CLC membrane transporters are unique in their ability to exchange anions for cations. Despite extensive study, there is no mechanistic model that fully explains their 2:1 Cl/H stoichiometric exchange mechanism. Here, we provide such a model. Using differential hydrogen-deuterium exchange mass spectrometry, cryo-EM structure determination, and molecular dynamics simulations, we uncovered conformational dynamics in CLC-ec1, a bacterial CLC homolog that has served as a paradigm for this family of transporters. Simulations based on a cryo-EM structure at pH 3 revealed critical steps in the transport mechanism, including release of Cl ions to the extracellular side, opening of the inner gate, and water wires that facilitate H transport. Surprisingly, these water wires occurred independently of Cl binding, prompting us to reassess the relationship between Cl binding and Cl/H coupling. Using isothermal titration calorimetry and quantitative flux assays on mutants with reduced Cl binding affinity, we conclude that, while Cl binding is necessary for coupling, even weak binding can support Cl/H coupling. By integrating our findings with existing literature, we establish a complete and efficient CLC 2:1 Cl/H exchange mechanism.
External links	Nat Commun / PubMed:41507156
Methods	EM (single particle)
Resolution	3.1 - 3.3 Å
Structure data	70242 9o95 EMDB-70242, PDB-9o95: Cryo-EM structure of CLC-ec1 at pH 7.5 Method: EM (single particle) / Resolution: 3.2 Å 70243 9o96 EMDB-70243, PDB-9o96: Cryo-EM structure of CLC-ec1 at pH 4.0 Method: EM (single particle) / Resolution: 3.2 Å 70244 9o97 EMDB-70244, PDB-9o97: Cryo-EM structure of CLC-ec1 at pH 3.0 Method: EM (single particle) / Resolution: 3.1 Å 70245 9o98 EMDB-70245, PDB-9o98: Cryo-EM structure of CLC-ec1 K131A at pH 7.5 Method: EM (single particle) / Resolution: 3.3 Å
Chemicals	ChemComp-CL: Unknown entry
Source	escherichia coli (E. coli)
Keywords	TRANSPORT PROTEIN / transmembrane protein cryo-EM Antiporter