6VWA

C-terminal regulatory domain of the chloride transporter KCC-1 from C. elegans

Summary for 6VWA

• Entry DOI: 10.2210/pdb6vwa/pdb
• Descriptor: K+/Cl-Cotransporter, TRIETHYLENE GLYCOL, DI(HYDROXYETHYL)ETHER, ... (5 entities in total)
• Functional Keywords: cation-chloride-cotransporter, slc transporter, cytosolic domain, transport protein
• Biological source: Caenorhabditis elegans
• Total number of polymer chains: 1
• Total formula weight: 46840.83

Authors

Zimanyi, C.M.,Cheung, J. (deposition date: 2020-02-19, release date: 2020-07-15, Last modification date: 2023-10-11)

Primary citation

Zimanyi, C.M.,Guo, M.,Mahmood, A.,Hendrickson, W.A.,Hirsh, D.,Cheung, J.
Structure of the Regulatory Cytosolic Domain of a Eukaryotic Potassium-Chloride Cotransporter.
Structure, 28:1051-1060.e4, 2020

PubMed Abstract: Cation-chloride cotransporters (CCCs) regulate the movement of chloride across membranes, controlling physiological processes from cell volume maintenance to neuronal signaling. Human CCCs are clinical targets for existing diuretics and potentially additional indications. Here, we report the X-ray crystal structure of the soluble C-terminal regulatory domain of a eukaryotic potassium-chloride cotransporter, Caenorhabditis elegans KCC-1. We observe a core α/β fold conserved among CCCs. Using structure-based sequence alignment, we analyze similarities and differences to the C-terminal domains of other CCC family members. We find that important regulatory motifs are in less-structured regions and residues important for dimerization are not widely conserved, suggesting that oligomerization and its effects may vary within the larger family. This snapshot of a eukaryotic KCC is a valuable starting point for the rational design of studies of cellular chloride regulation.

PubMed: 32679039
DOI: 10.1016/j.str.2020.06.009

Experimental method

X-RAY DIFFRACTION (2.196 Å)