1jvm
From Proteopedia
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| - | [[Image:1jvm.gif|left|200px]] | + | [[Image:1jvm.gif|left|200px]] |
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| - | '''KCSA POTASSIUM CHANNEL WITH TBA (TETRABUTYLAMMONIUM) AND RUBIDIUM''' | + | {{Structure |
| + | |PDB= 1jvm |SIZE=350|CAPTION= <scene name='initialview01'>1jvm</scene>, resolution 2.8Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=RB:RUBIDIUM+ION'>RB</scene> and <scene name='pdbligand=TBA:TETRABUTYLAMMONIUM ION'>TBA</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''KCSA POTASSIUM CHANNEL WITH TBA (TETRABUTYLAMMONIUM) AND RUBIDIUM''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1JVM is a [ | + | 1JVM is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_lividans Streptomyces lividans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JVM OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11689935 11689935] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Streptomyces lividans]] | [[Category: Streptomyces lividans]] | ||
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[[Category: potassium channel]] | [[Category: potassium channel]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:09:04 2008'' |
Revision as of 10:09, 20 March 2008
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| , resolution 2.8Å | |||||||
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| Ligands: | and | ||||||
| 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
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