5fim: Difference between revisions
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The | ==The structure of Kbp.K from E. coli== | ||
<StructureSection load='5fim' size='340' side='right' caption='[[5fim]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5fim]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FIM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5FIM FirstGlance]. <br> | |||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5fim FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fim OCA], [http://pdbe.org/5fim PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fim RCSB], [http://www.ebi.ac.uk/pdbsum/5fim PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Escherichia coli possesses a number of specific K(+) influx and efflux systems that maintain an appropriate intracellular K(+) concentration. Although regulatory mechanisms have been identified for a number of these transport systems, the exact mechanism through which K(+) concentration is sensed in the cell remains unknown. In this work we show that Kbp (K(+) binding protein, formerly YgaU), a soluble 16-kDa cytoplasmic protein from Escherichia coli, is a highly specific K(+) binding protein and is required for normal growth in the presence of high levels of external K(+). Kbp binds a single potassium ion with high specificity over Na(+) and other metal ions found in biological systems, although, in common with K(+) transporters, it also binds Rb(+) and Cs(+). Dissection of the K(+) binding determinants of Kbp suggests a mechanism through which Kbp is able to sense changes in K(+) concentration over the relevant range of intracellular K(+) concentrations. | |||
The Potassium Binding Protein Kbp Is a Cytoplasmic Potassium Sensor.,Ashraf KU, Josts I, Mosbahi K, Kelly SM, Byron O, Smith BO, Walker D Structure. 2016 May 3;24(5):741-9. doi: 10.1016/j.str.2016.03.017. Epub 2016 Apr , 21. PMID:27112601<ref>PMID:27112601</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 5fim" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Ashraf, K U]] | |||
[[Category: Smith, B O]] | |||
[[Category: Walker, D]] | [[Category: Walker, D]] | ||
[[Category: | [[Category: Potassium binding]] | ||
[[Category: | [[Category: Unknown function]] | ||
[[Category: Ygau]] | |||
Revision as of 03:41, 11 May 2016
The structure of Kbp.K from E. coli
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