1QRQ
STRUCTURE OF A VOLTAGE-DEPENDENT K+ CHANNEL BETA SUBUNIT
Summary for 1QRQ
| Entry DOI | 10.2210/pdb1qrq/pdb |
| Descriptor | PROTEIN (KV BETA2 PROTEIN), NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE (3 entities in total) |
| Functional Keywords | tim barrel, aldo-keto reductase, potassium channel subunit, voltage-dependent potassium channel, metal transport |
| Biological source | Rattus norvegicus (Norway rat) |
| Cellular location | Cytoplasm : P62483 |
| Total number of polymer chains | 4 |
| Total formula weight | 148397.34 |
| Authors | Gulbis, J.M.,Mann, S.,MacKinnon, R. (deposition date: 1999-06-15, release date: 1999-10-27, Last modification date: 2024-02-14) |
| Primary citation | Gulbis, J.M.,Mann, S.,MacKinnon, R. Structure of a voltage-dependent K+ channel beta subunit. Cell(Cambridge,Mass.), 97:943-952, 1999 Cited by PubMed Abstract: The integral membrane subunits of many voltage-dependent potassium channels are associated with an additional protein known as the beta subunit. One function of beta subunits is to modify K+ channel gating. We have determined the structure of the conserved core of mammalian beta subunits by X-ray crystallography at 2.8 A resolution. Like the integral membrane component of K+ channels, beta subunits form a four-fold symmetric structure. Each subunit is an oxidoreductase enzyme complete with a nicotinamide co-factor in its active site. Several structural features of the enzyme active site, including its location with respect to the four-fold axis, imply that it may interact directly or indirectly with the K+ channel's voltage sensor. This structure suggests a mechanism for coupling membrane electrical excitability directly to chemistry of the cell. PubMed: 10399921DOI: 10.1016/S0092-8674(00)80805-3 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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