6q7q: Difference between revisions
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<StructureSection load='6q7q' size='340' side='right'caption='[[6q7q]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='6q7q' size='340' side='right'caption='[[6q7q]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6q7q]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6Q7Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6Q7Q FirstGlance]. <br> | <table><tr><td colspan='2'>[[6q7q]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/'pyrococcus_shinkaii' 'pyrococcus shinkaii']. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6Q7Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6Q7Q FirstGlance]. <br> | ||
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MHS:N1-METHYLATED+HISTIDINE'>MHS</scene></td></tr> | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MHS:N1-METHYLATED+HISTIDINE'>MHS</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PH0459 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=53953 'Pyrococcus shinkaii'])</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=6q7q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6q7q OCA], [http://pdbe.org/6q7q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6q7q RCSB], [http://www.ebi.ac.uk/pdbsum/6q7q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6q7q ProSAT]</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=6q7q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6q7q OCA], [http://pdbe.org/6q7q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6q7q RCSB], [http://www.ebi.ac.uk/pdbsum/6q7q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6q7q ProSAT]</span></td></tr> | ||
</table> | </table> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Pyrococcus shinkaii]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Levy, C W]] | [[Category: Levy, C W]] | ||
[[Category: Computationally designed enzyme]] | [[Category: Computationally designed enzyme]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
Revision as of 10:40, 26 June 2019
Crystal structure of OE1.3Crystal structure of OE1.3
Structural highlights
Publication Abstract from PubMedThe combination of computational design and laboratory evolution is a powerful and potentially versatile strategy for the development of enzymes with new functions(1-4). However, the limited functionality presented by the genetic code restricts the range of catalytic mechanisms that are accessible in designed active sites. Inspired by mechanistic strategies from small-molecule organocatalysis(5), here we report the generation of a hydrolytic enzyme that uses Ndelta-methylhistidine as a non-canonical catalytic nucleophile. Histidine methylation is essential for catalytic function because it prevents the formation of unreactive acyl-enzyme intermediates, which has been a long-standing challenge when using canonical nucleophiles in enzyme design(6-10). Enzyme performance was optimized using directed evolution protocols adapted to an expanded genetic code, affording a biocatalyst capable of accelerating ester hydrolysis with greater than 9,000-fold increased efficiency over free Ndelta-methylhistidine in solution. Crystallographic snapshots along the evolutionary trajectory highlight the catalytic devices that are responsible for this increase in efficiency. Ndelta-methylhistidine can be considered to be a genetically encodable surrogate of the widely employed nucleophilic catalyst dimethylaminopyridine(11), and its use will create opportunities to design and engineer enzymes for a wealth of valuable chemical transformations. Design and evolution of an enzyme with a non-canonical organocatalytic mechanism.,Burke AJ, Lovelock SL, Frese A, Crawshaw R, Ortmayer M, Dunstan M, Levy C, Green AP Nature. 2019 May 27. pii: 10.1038/s41586-019-1262-8. doi:, 10.1038/s41586-019-1262-8. PMID:31132786[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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