View source for 6nw4


==Evolution of a computationally designed Kemp eliminase==
<StructureSection load='6nw4' size='340' side='right'caption='[[6nw4]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6nw4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharolobus_solfataricus_P2 Saccharolobus solfataricus P2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6NW4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6NW4 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]] 3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=6NT:6-NITROBENZOTRIAZOLE'>6NT</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=6nw4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6nw4 OCA], [https://pdbe.org/6nw4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6nw4 RCSB], [https://www.ebi.ac.uk/pdbsum/6nw4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6nw4 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/TRPC_SACS2 TRPC_SACS2] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Temperature influences the reaction kinetics and evolvability of all enzymes. To understand how evolution shapes the thermodynamic drivers of catalysis, we optimized the modest activity of a computationally designed enzyme for an elementary proton-transfer reaction by nearly 4 orders of magnitude over 9 rounds of mutagenesis and screening. As theorized for primordial enzymes, the catalytic effects of the original design were almost entirely enthalpic in origin, as were the rate enhancements achieved by laboratory evolution. However, the large reductions in DeltaH() were partially offset by a decrease in TDeltaS() and unexpectedly accompanied by a negative activation heat capacity, signaling strong adaptation to the operating temperature. These findings echo reports of temperature-dependent activation parameters for highly evolved natural enzymes and are relevant to explanations of enzymatic catalysis and adaptation to changing thermal environments.

Emergence of a Negative Activation Heat Capacity during Evolution of a Designed Enzyme.,Bunzel HA, Kries H, Marchetti L, Zeymer C, Mittl PRE, Mulholland AJ, Hilvert D J Am Chem Soc. 2019 Jul 19. doi: 10.1021/jacs.9b02731. PMID:31282667<ref>PMID:31282667</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6nw4" style="background-color:#fffaf0;"></div>

==See Also==
*[[IGPS 3D structures|IGPS 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharolobus solfataricus P2]]
[[Category: Bunzel A]]
[[Category: Hilvert D]]
[[Category: Mittl P]]