View source for 5od1


==Structure of the engineered metalloesterase MID1sc10 complexed with a phosphonate transition state analogue==
<StructureSection load='5od1' size='340' side='right'caption='[[5od1]], [[Resolution|resolution]] 1.34&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5od1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OD1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5OD1 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]] 1.34&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=9RQ:[2-oxidanylidene-7-[oxidanyl-[(1~{S})-1-phenylethyl]phosphoryl]oxy-chromen-4-yl]methanesulfonic+acid'>9RQ</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=5od1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5od1 OCA], [https://pdbe.org/5od1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5od1 RCSB], [https://www.ebi.ac.uk/pdbsum/5od1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5od1 ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
Primordial sequence signatures in modern proteins imply ancestral origins tracing back to simple peptides. Although short peptides seldom adopt unique folds, metal ions might have templated their assembly into higher-order structures in early evolution and imparted useful chemical reactivity. Recapitulating such a biogenetic scenario, we have combined design and laboratory evolution to transform a zinc-binding peptide into a globular enzyme capable of accelerating ester cleavage with exacting enantiospecificity and high catalytic efficiency (k cat/K M ~ 10(6) M(-1) s(-1)). The simultaneous optimization of structure and function in a naive peptide scaffold not only illustrates a plausible enzyme evolutionary pathway from the distant past to the present but also proffers exciting future opportunities for enzyme design and engineering.

Evolution of a highly active and enantiospecific metalloenzyme from short peptides.,Studer S, Hansen DA, Pianowski ZL, Mittl PRE, Debon A, Guffy SL, Der BS, Kuhlman B, Hilvert D Science. 2018 Dec 14;362(6420):1285-1288. doi: 10.1126/science.aau3744. PMID:30545884<ref>PMID:30545884</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5od1" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Synthetic construct]]
[[Category: Hansen DA]]
[[Category: Hilvert D]]
[[Category: Mittl PRE]]
[[Category: Studer S]]