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4fzo
From Proteopedia
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| - | + | ==Crystal Structure of the apo-form uranyl binding protein== | |
| - | + | <StructureSection load='4fzo' size='340' side='right' caption='[[4fzo]], [[Resolution|resolution]] 1.30Å' scene=''> | |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4fzo]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Metth Metth]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FZO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FZO FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4fzp|4fzp]]</td></tr> | ||
| + | <tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MTH_1690 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=187420 METTH])</td></tr> | ||
| + | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4fzo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fzo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4fzo RCSB], [http://www.ebi.ac.uk/pdbsum/4fzo PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Uranyl (UO2(2+)), the predominant aerobic form of uranium, is present in the ocean at a concentration of ~3.2 parts per 10(9) (13.7 nM); however, the successful enrichment of uranyl from this vast resource has been limited by the high concentrations of metal ions of similar size and charge, which makes it difficult to design a binding motif that is selective for uranyl. Here we report the design and rational development of a uranyl-binding protein using a computational screening process in the initial search for potential uranyl-binding sites. The engineered protein is thermally stable and offers very high affinity and selectivity for uranyl with a Kd of 7.4 femtomolar (fM) and >10,000-fold selectivity over other metal ions. We also demonstrated that the uranyl-binding protein can repeatedly sequester 30-60% of the uranyl in synthetic sea water. The chemical strategy employed here may be applied to engineer other selective metal-binding proteins for biotechnology and remediation applications. | ||
| - | + | A protein engineered to bind uranyl selectively and with femtomolar affinity.,Zhou L, Bosscher M, Zhang C, Ozcubukcu S, Zhang L, Zhang W, Li CJ, Liu J, Jensen MP, Lai L, He C Nat Chem. 2014 Mar;6(3):236-41. doi: 10.1038/nchem.1856. Epub 2014 Jan 26. PMID:24557139<ref>PMID:24557139</ref> | |
| - | + | ||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Metth]] | ||
[[Category: He, C.]] | [[Category: He, C.]] | ||
[[Category: Zhang, L.]] | [[Category: Zhang, L.]] | ||
Revision as of 07:06, 21 May 2014
Crystal Structure of the apo-form uranyl binding protein
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Categories: Metth | He, C. | Zhang, L. | Zhou, L. | Unknown function | Uranyl | Uranyl binding
