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1qrq
From Proteopedia
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|PDB= 1qrq |SIZE=350|CAPTION= <scene name='initialview01'>1qrq</scene>, resolution 2.80Å | |PDB= 1qrq |SIZE=350|CAPTION= <scene name='initialview01'>1qrq</scene>, resolution 2.80Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=NDP:NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE'>NDP</scene> | + | |LIGAND= <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qrq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qrq OCA], [http://www.ebi.ac.uk/pdbsum/1qrq PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qrq RCSB]</span> | ||
}} | }} | ||
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[[Category: MacKinnon, R.]] | [[Category: MacKinnon, R.]] | ||
[[Category: Mann, S.]] | [[Category: Mann, S.]] | ||
| - | [[Category: NDP]] | ||
[[Category: aldo-keto reductase]] | [[Category: aldo-keto reductase]] | ||
[[Category: metal transport]] | [[Category: metal transport]] | ||
| Line 32: | Line 34: | ||
[[Category: voltage-dependent potassium channel]] | [[Category: voltage-dependent potassium channel]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:18:05 2008'' |
Revision as of 20:18, 30 March 2008
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| , resolution 2.80Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF A VOLTAGE-DEPENDENT K+ CHANNEL BETA SUBUNIT
Overview
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.
About this Structure
1QRQ is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Structure of a voltage-dependent K+ channel beta subunit., Gulbis JM, Mann S, MacKinnon R, Cell. 1999 Jun 25;97(7):943-52. PMID:10399921
Page seeded by OCA on Sun Mar 30 23:18:05 2008
