1zwi
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1zwi |SIZE=350|CAPTION= <scene name='initialview01'>1zwi</scene>, resolution 2.50Å | |PDB= 1zwi |SIZE=350|CAPTION= <scene name='initialview01'>1zwi</scene>, resolution 2.50Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=DGA:DIACYL+GLYCEROL'>DGA</scene>, <scene name='pdbligand=F09:NONAN-1-OL'>F09</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= kcsA, skc1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1916 Streptomyces lividans]) | |GENE= kcsA, skc1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1916 Streptomyces lividans]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1zwi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zwi OCA], [http://www.ebi.ac.uk/pdbsum/1zwi PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1zwi RCSB]</span> | ||
}} | }} | ||
| Line 30: | Line 33: | ||
[[Category: Roux, B.]] | [[Category: Roux, B.]] | ||
[[Category: Zhao, Y.]] | [[Category: Zhao, Y.]] | ||
| - | [[Category: | + | [[Category: potassium ion channel]] |
| - | [[Category: | + | [[Category: transmembrane protein]] |
| - | + | [[Category: x-ray crystallography]] | |
| - | [[Category: x-ray crystallography | + | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:42:34 2008'' |
Revision as of 22:42, 30 March 2008
| |||||||
| , resolution 2.50Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Gene: | kcsA, skc1 (Streptomyces lividans) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure of mutant KcsA potassium channel
Overview
We show that in the potassium channel KcsA, proton-dependent activation is followed by an inactivation process similar to C-type inactivation, and this process is suppressed by an E71A mutation in the pore helix. EPR spectroscopy demonstrates that the inner gate opens maximally at low pH regardless of the magnitude of the single-channel-open probability, implying that stationary gating originates mostly from rearrangements at the selectivity filter. Two E71A crystal structures obtained at 2.5 A reveal large structural excursions of the selectivity filter during ion conduction and provide a glimpse of the range of conformations available to this region of the channel during gating. These data establish a mechanistic basis for the role of the selectivity filter during channel activation and inactivation.
About this Structure
1ZWI is a Single protein structure of sequence from Mus musculus and Streptomyces lividans. Full crystallographic information is available from OCA.
Reference
Molecular determinants of gating at the potassium-channel selectivity filter., Cordero-Morales JF, Cuello LG, Zhao Y, Jogini V, Cortes DM, Roux B, Perozo E, Nat Struct Mol Biol. 2006 Apr;13(4):311-8. Epub 2006 Mar 12. PMID:16532009
Page seeded by OCA on Mon Mar 31 01:42:34 2008
