6nw4: Difference between revisions
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==Evolution of a computationally designed Kemp eliminase== | |||
<StructureSection load='6nw4' size='340' side='right'caption='[[6nw4]], [[Resolution|resolution]] 3.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6nw4]] is a 1 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6NW4 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=6NT:6-NITROBENZOTRIAZOLE'>6NT</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Indole-3-glycerol-phosphate_synthase Indole-3-glycerol-phosphate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.48 4.1.1.48] </span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6nw4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6nw4 OCA], [http://pdbe.org/6nw4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6nw4 RCSB], [http://www.ebi.ac.uk/pdbsum/6nw4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6nw4 ProSAT]</span></td></tr> | |||
</table> | |||
<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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6nw4" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Indole-3-glycerol-phosphate synthase]] | |||
[[Category: Large Structures]] | |||
[[Category: Bunzel, A]] | |||
[[Category: Hilvert, D]] | |||
[[Category: Mittl, P]] | |||
[[Category: Biosynthetic protein]] | |||
[[Category: Evolution]] | |||
[[Category: Kemp elimination]] | |||
Revision as of 09:17, 24 July 2019
Evolution of a computationally designed Kemp eliminaseEvolution of a computationally designed Kemp eliminase
Structural highlights
Publication Abstract from PubMedTemperature 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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