2atk: Difference between revisions
No edit summary |
No edit summary |
||
| Line 4: | Line 4: | ||
|PDB= 2atk |SIZE=350|CAPTION= <scene name='initialview01'>2atk</scene>, resolution 2.5Å | |PDB= 2atk |SIZE=350|CAPTION= <scene name='initialview01'>2atk</scene>, resolution 2.5Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=F09:NONAN-1-OL'>F09</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1zwi|1ZWI]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2atk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2atk OCA], [http://www.ebi.ac.uk/pdbsum/2atk PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2atk RCSB]</span> | |||
}} | }} | ||
| Line 30: | Line 33: | ||
[[Category: Roux, B.]] | [[Category: Roux, B.]] | ||
[[Category: Zhao, Y.]] | [[Category: Zhao, Y.]] | ||
[[Category: k+ channel]] | [[Category: k+ channel]] | ||
[[Category: mutant kcsa]] | [[Category: mutant kcsa]] | ||
[[Category: protein-antibody fab complex]] | [[Category: protein-antibody fab complex]] | ||
''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 01:57:09 2008'' | ||
Revision as of 01:57, 31 March 2008
| |||||||
| , resolution 2.5Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Related: | 1ZWI
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure of a mutant KcsA K+ channel
OverviewOverview
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 StructureAbout this Structure
2ATK is a Single protein structure of sequence from Mus musculus and Streptomyces lividans. Full crystallographic information is available from OCA.
ReferenceReference
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 01:57:09 2008