1jvm

KCSA POTASSIUM CHANNEL WITH TBA (TETRABUTYLAMMONIUM) AND RUBIDIUM

spinqualitylabelsall models 1jvm, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1jvm is a 4 chain structure with sequence from "actinomyces_lividans"_krasil'nikov_et_al._1965 "actinomyces lividans" krasil'nikov et al. 1965. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: RB, TBA Related: 1j95, 1bl8 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [KCSA_STRLI] Acts as a pH-gated potassium ion channel; changing the cytosolic pH from 7 to 4 opens the channel, although it is not clear if this is the physiological stimulus for channel opening. Monovalent cation preference is K(+) > Rb(+) > NH4(+) >> Na(+) > Li(+). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Potassium Channel

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