3ORG

Crystal Structure of a eukaryotic CLC transporter

Summary for 3ORG

• Entry DOI: 10.2210/pdb3org/pdb
• Descriptor: CmCLC, CHLORIDE ION (2 entities in total)
• Functional Keywords: clc, transporter, transport protein
• Biological source: Cyanidioschyzon merolae
• Total number of polymer chains: 4
• Total formula weight: 276900.28

Authors

Feng, L.,MacKinnon, R. (deposition date: 2010-09-07, release date: 2010-10-06, Last modification date: 2024-02-21)

Primary citation

Feng, L.,Campbell, E.B.,Hsiung, Y.,MacKinnon, R.
Structure of a eukaryotic CLC transporter defines an intermediate state in the transport cycle.
Science, 330:635-641, 2010

PubMed Abstract: CLC proteins transport chloride (Cl(-)) ions across cell membranes to control the electrical potential of muscle cells, transfer electrolytes across epithelia, and control the pH and electrolyte composition of intracellular organelles. Some members of this protein family are Cl(-) ion channels, whereas others are secondary active transporters that exchange Cl(-) ions and protons (H(+)) with a 2:1 stoichiometry. We have determined the structure of a eukaryotic CLC transporter at 3.5 angstrom resolution. Cytoplasmic cystathionine beta-synthase (CBS) domains are strategically positioned to regulate the ion-transport pathway, and many disease-causing mutations in human CLCs reside on the CBS-transmembrane interface. Comparison with prokaryotic CLC shows that a gating glutamate residue changes conformation and suggests a basis for 2:1 Cl(-)/H(+) exchange and a simple mechanistic connection between CLC channels and transporters.

PubMed: 20929736
DOI: 10.1126/science.1195230

Experimental method

X-RAY DIFFRACTION (3.5 Å)