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| - | | + | #REDIRECT [[7pvc]] This PDB entry is obsolete and replaced by 7pvc |
| - | ==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 with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. 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], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5fim ProSAT]</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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| - | 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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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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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: Bacillus coli migula 1895]]
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| - | [[Category: Large Structures]]
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| - | [[Category: Ashraf, K U]]
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| - | [[Category: Smith, B O]]
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| - | [[Category: Walker, D]]
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| - | [[Category: Potassium binding]]
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| - | [[Category: Unknown function]]
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| - | [[Category: Ygau]]
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