1jvm
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1jvm |SIZE=350|CAPTION= <scene name='initialview01'>1jvm</scene>, resolution 2.8Å | |PDB= 1jvm |SIZE=350|CAPTION= <scene name='initialview01'>1jvm</scene>, resolution 2.8Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=RB:RUBIDIUM+ION'>RB</scene> | + | |LIGAND= <scene name='pdbligand=RB:RUBIDIUM+ION'>RB</scene>, <scene name='pdbligand=TBA:TETRABUTYLAMMONIUM+ION'>TBA</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1j95|1J95]], [[1bl8|1BL8]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jvm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jvm OCA], [http://www.ebi.ac.uk/pdbsum/1jvm PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1jvm RCSB]</span> | ||
}} | }} | ||
| Line 25: | Line 28: | ||
[[Category: Morais-Cabral, J H.]] | [[Category: Morais-Cabral, J H.]] | ||
[[Category: Zhou, Y.]] | [[Category: Zhou, Y.]] | ||
| - | [[Category: RB]] | ||
| - | [[Category: TBA]] | ||
[[Category: membrane protein]] | [[Category: membrane protein]] | ||
[[Category: metal transport]] | [[Category: metal transport]] | ||
[[Category: potassium channel]] | [[Category: 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 21:39:43 2008'' |
Revision as of 18:39, 30 March 2008
| |||||||
| , resolution 2.8Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Related: | 1J95, 1BL8
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
KCSA POTASSIUM CHANNEL WITH TBA (TETRABUTYLAMMONIUM) AND RUBIDIUM
Overview
The K+ selectivity filter catalyses the dehydration, transfer and rehydration of a K+ ion in about ten nanoseconds. This physical process is central to the production of electrical signals in biology. Here we show how nearly diffusion-limited rates are achieved, by analysing ion conduction and the corresponding crystallographic ion distribution in the selectivity filter of the KcsA K+ channel. Measurements with K+ and its slightly larger analogue, Rb+, lead us to conclude that the selectivity filter usually contains two K+ ions separated by one water molecule. The two ions move in a concerted fashion between two configurations, K+-water-K+-water (1,3 configuration) and water-K+-water-K+ (2,4 configuration), until a third ion enters, displacing the ion on the opposite side of the queue. For K+, the energy difference between the 1,3 and 2,4 configurations is close to zero, the condition of maximum conduction rate. The energetic balance between these configurations is a clear example of evolutionary optimization of protein function.
About this Structure
1JVM is a Single protein structure of sequence from Streptomyces lividans. Full crystallographic information is available from OCA.
Reference
Energetic optimization of ion conduction rate by the K+ selectivity filter., Morais-Cabral JH, Zhou Y, MacKinnon R, Nature. 2001 Nov 1;414(6859):37-42. PMID:11689935
Page seeded by OCA on Sun Mar 30 21:39:43 2008
