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4MQX

CLC-ec1 Fab Complex Cysless A399C-A432C mutant

Summary for 4MQX
Entry DOI10.2210/pdb4mqx/pdb
Related1OTS
DescriptorH(+)/Cl(-) exchange transporter ClcA, ecCLC, ERIC, ... (4 entities in total)
Functional Keywordsalpha helical transmembrane protein, cl/h antiporter, metal transport, membrane protein
Biological sourceEscherichia coli
More
Cellular locationCell inner membrane; Multi-pass membrane protein (Probable): P37019
Total number of polymer chains6
Total formula weight193250.02
Authors
Basilio, D.,Noack, K.,Picollo, A.,Accardi, A. (deposition date: 2013-09-16, release date: 2014-04-16, Last modification date: 2024-11-27)
Primary citationBasilio, D.,Noack, K.,Picollo, A.,Accardi, A.
Conformational changes required for H(+)/Cl(-) exchange mediated by a CLC transporter.
Nat.Struct.Mol.Biol., 21:456-463, 2014
Cited by
PubMed Abstract: CLC-type exchangers mediate transmembrane Cl(-) transport. Mutations altering their gating properties cause numerous genetic disorders. However, their transport mechanism remains poorly understood. In conventional models, two gates alternatively expose substrates to the intra- or extracellular solutions. A glutamate was identified as the only gate in the CLCs, suggesting that CLCs function by a nonconventional mechanism. Here we show that transport in CLC-ec1, a prokaryotic homolog, is inhibited by cross-links constraining movement of helix O far from the transport pathway. Cross-linked CLC-ec1 adopts a wild-type-like structure, indicating stabilization of a native conformation. Movements of helix O are transduced to the ion pathway via a direct contact between its C terminus and a tyrosine that is a constitutive element of the second gate of CLC transporters. Therefore, the CLC exchangers have two gates that are coupled through conformational rearrangements outside the ion pathway.
PubMed: 24747941
DOI: 10.1038/nsmb.2814
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.516 Å)
Structure validation

237735

数据于2025-06-18公开中

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