2JA3

Cytoplasmic Domain of the Human Chloride Transporter ClC-5 in complex with ADP

Summary for 2JA3

• Entry DOI: 10.2210/pdb2ja3/pdb
• Descriptor: CHLORIDE CHANNEL PROTEIN 5, ADENOSINE-5'-DIPHOSPHATE (2 entities in total)
• Functional Keywords: membrane, chloride, transport, cbs domain, clc, chloride channel, disease mutation, ionic channel, ion transport, transmembrane, transport protein, chloride transporter, voltage-gated channel
• Biological source: HOMO SAPIENS (HUMAN)
• Total number of polymer chains: 6
• Total formula weight: 129022.02

Authors

Meyer, S.,Savaresi, S.,Forster, I.C.,Dutzler, R. (deposition date: 2006-11-21, release date: 2007-01-04, Last modification date: 2024-05-08)

Primary citation

Meyer, S.,Savaresi, S.,Forster, I.C.,Dutzler, R.
Nucleotide Recognition by the Cytoplasmic Domain of the Human Chloride Transporter Clc-5
Nat.Struct.Mol.Biol., 14:60-, 2006

PubMed Abstract: The ubiquitous CBS domains, which are found as part of cytoplasmic domains in the ClC family of chloride channels and transporters, have previously been identified as building blocks for regulatory nucleotide-binding sites. Here we report the structures of the cytoplasmic domain of the human transporter ClC-5 in complex with ATP and ADP. The nucleotides bind to a specific site in the protein. As determined by equilibrium dialysis, the affinities for ATP, ADP and AMP are in the high micromolar range. Point mutations that interfere with nucleotide binding change the transport behavior of a ClC-5 mutant expressed in Xenopus laevis oocytes. Our results establish the structural and energetic basis for the interaction of ClC-5 with nucleotides and provide a framework for future investigations.

PubMed: 17195847
DOI: 10.1038/NSMB1188

Experimental method

X-RAY DIFFRACTION (3.05 Å)