4fzo

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4fzo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fzo OCA], [https://pdbe.org/4fzo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fzo RCSB], [https://www.ebi.ac.uk/pdbsum/4fzo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fzo ProSAT]</span></td></tr>

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== 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 &gt;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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

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