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5fim

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'''Unreleased structure'''
 
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The entry 5fim is ON HOLD until Paper Publication
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==The structure of Kbp.K from E. coli==
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<StructureSection load='5fim' size='340' side='right' caption='[[5fim]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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== Structural highlights ==
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<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>
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</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>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Authors: SMITH, B.O., ASHRAF, K.U., WALKER, D.
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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>
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Description: The structure of Kbp.K from E. coli
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 5fim" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Ashraf, K U]]
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[[Category: Smith, B O]]
[[Category: Walker, D]]
[[Category: Walker, D]]
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[[Category: Smith, B.O]]
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[[Category: Potassium binding]]
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[[Category: Ashraf, K.U]]
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[[Category: Unknown function]]
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[[Category: Ygau]]

Revision as of 03:41, 11 May 2016

The structure of Kbp.K from E. coli

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