View source for 4fzp


==Crystal Structure of the uranyl binding protein complexed with uranyl==
<StructureSection load='4fzp' size='340' side='right'caption='[[4fzp]], [[Resolution|resolution]] 1.29&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4fzp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanothermobacter_thermautotrophicus_str._Delta_H Methanothermobacter thermautotrophicus str. Delta H]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FZP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FZP FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.29&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IUM:URANYL+(VI)+ION'>IUM</scene></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=4fzp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fzp OCA], [https://pdbe.org/4fzp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fzp RCSB], [https://www.ebi.ac.uk/pdbsum/4fzp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fzp ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/O27725_METTH O27725_METTH] 
<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 &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>
</div>
<div class="pdbe-citations 4fzp" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Methanothermobacter thermautotrophicus str. Delta H]]
[[Category: He C]]
[[Category: Zhang L]]
[[Category: Zhou L]]