7k4y
From Proteopedia
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==Crystal structure of Kemp Eliminase HG3.17 at 343 K== | ==Crystal structure of Kemp Eliminase HG3.17 at 343 K== | ||
| - | <StructureSection load='7k4y' size='340' side='right'caption='[[7k4y]]' scene=''> | + | <StructureSection load='7k4y' size='340' side='right'caption='[[7k4y]], [[Resolution|resolution]] 1.80Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7K4Y OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7K4Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7K4Y FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</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=7k4y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7k4y OCA], [https://pdbe.org/7k4y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7k4y RCSB], [https://www.ebi.ac.uk/pdbsum/7k4y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7k4y ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The advent of biocatalysts designed computationally and optimized by laboratory evolution provides an opportunity to explore molecular strategies for augmenting catalytic function. Applying a suite of nuclear magnetic resonance, crystallography, and stopped-flow techniques to an enzyme designed for an elementary proton transfer reaction, we show how directed evolution gradually altered the conformational ensemble of the protein scaffold to populate a narrow, highly active conformational ensemble and accelerate this transformation by nearly nine orders of magnitude. Mutations acquired during optimization enabled global conformational changes, including high-energy backbone rearrangements, that cooperatively organized the catalytic base and oxyanion stabilizer, thus perfecting transition-state stabilization. The development of protein catalysts for many chemical transformations could be facilitated by explicitly sampling conformational substates during design and specifically stabilizing productive substates over all unproductive conformations. | ||
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| + | How directed evolution reshapes the energy landscape in an enzyme to boost catalysis.,Otten R, Padua RAP, Bunzel HA, Nguyen V, Pitsawong W, Patterson M, Sui S, Perry SL, Cohen AE, Hilvert D, Kern D Science. 2020 Dec 18;370(6523):1442-1446. doi: 10.1126/science.abd3623. Epub 2020, Nov 19. PMID:33214289<ref>PMID:33214289</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7k4y" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Kemp eliminase|Kemp eliminase]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
Crystal structure of Kemp Eliminase HG3.17 at 343 K
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Categories: Large Structures | Bunzel A | Cohen AE | Hilvert D | Kern D | Nguyen V | Otten R | Padua RAP | Patterson M | Perry SL | Pitsawong W | Sui S
