1EXB

STRUCTURE OF THE CYTOPLASMIC BETA SUBUNIT-T1 ASSEMBLY OF VOLTAGE-DEPENDENT K CHANNELS

Summary for 1EXB

• Entry DOI: 10.2210/pdb1exb/pdb
• Related: 1qrq 1t1d
• Descriptor: KV BETA2 PROTEIN, POTASSIUM CHANNEL KV1.1, NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, ... (4 entities in total)
• Functional Keywords: ion channel, oxidoreductase, beta subunit, metal transport
• Biological source: Rattus norvegicus (Norway rat); More
• Cellular location: Cytoplasm (Potential): P62483; Membrane; Multi-pass membrane protein: P10499
• Total number of polymer chains: 2
• Total formula weight: 50314.26

Authors

Gulbis, J.M.,Zhou, M.,Mann, S.,MacKinnon, R. (deposition date: 2000-05-02, release date: 2000-07-19, Last modification date: 2024-02-07)

Primary citation

Gulbis, J.M.,Zhou, M.,Mann, S.,MacKinnon, R.
Structure of the cytoplasmic beta subunit-T1 assembly of voltage-dependent K+ channels.
Science, 289:123-127, 2000

PubMed Abstract: The structure of the cytoplasmic assembly of voltage-dependent K+ channels was solved by x-ray crystallography at 2.1 angstrom resolution. The assembly includes the cytoplasmic (T1) domain of the integral membrane alpha subunit together with the oxidoreductase beta subunit in a fourfold symmetric T1(4)beta4 complex. An electrophysiological assay showed that this complex is oriented with four T1 domains facing the transmembrane pore and four beta subunits facing the cytoplasm. The transmembrane pore communicates with the cytoplasm through lateral, negatively charged openings above the T1(4)beta4 complex. The inactivation peptides of voltage-dependent K(+) channels reach their site of action by entering these openings.

PubMed: 10884227
DOI: 10.1126/science.289.5476.123

Experimental method

X-RAY DIFFRACTION (2.1 Å)