6c7h: Difference between revisions
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<StructureSection load='6c7h' size='340' side='right' caption='[[6c7h]], [[Resolution|resolution]] 2.43Å' scene=''> | <StructureSection load='6c7h' size='340' side='right' caption='[[6c7h]], [[Resolution|resolution]] 2.43Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6c7h]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6C7H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6C7H FirstGlance]. <br> | <table><tr><td colspan='2'>[[6c7h]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Synthetic_construct_sequences Synthetic construct sequences]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6C7H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6C7H FirstGlance]. <br> | ||
</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=6c7h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6c7h OCA], [http://pdbe.org/6c7h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6c7h RCSB], [http://www.ebi.ac.uk/pdbsum/6c7h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6c7h ProSAT]</span></td></tr> | </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=6c7h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6c7h OCA], [http://pdbe.org/6c7h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6c7h RCSB], [http://www.ebi.ac.uk/pdbsum/6c7h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6c7h ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Developments in computational chemistry, bioinformatics, and laboratory evolution have facilitated the de novo design and catalytic optimization of enzymes. Besides creating useful catalysts, the generation and iterative improvement of designed enzymes can provide valuable insight into the interplay between the many phenomena that have been suggested to contribute to catalysis. In this work, we follow changes in conformational sampling, electrostatic preorganization, and quantum tunneling along the evolutionary trajectory of a designed Kemp eliminase. We observe that in the Kemp Eliminase KE07, instability of the designed active site leads to the emergence of two additional active site configurations. Evolutionary conformational selection then gradually stabilizes the most efficient configuration, leading to an improved enzyme. This work exemplifies the link between conformational plasticity and evolvability and demonstrates that residues remote from the active sites of enzymes play crucial roles in controlling and shaping the active site for efficient catalysis. | |||
The evolution of multiple active site configurations in a designed enzyme.,Hong NS, Petrovic D, Lee R, Gryn'ova G, Purg M, Saunders J, Bauer P, Carr PD, Lin CY, Mabbitt PD, Zhang W, Altamore T, Easton C, Coote ML, Kamerlin SCL, Jackson CJ Nat Commun. 2018 Sep 25;9(1):3900. doi: 10.1038/s41467-018-06305-y. PMID:30254369<ref>PMID:30254369</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6c7h" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Synthetic construct sequences]] | |||
[[Category: Carr, P D]] | [[Category: Carr, P D]] | ||
[[Category: Hong, N S]] | [[Category: Hong, N S]] | ||
Revision as of 12:44, 13 February 2019
Directed evolutionary changes in Kemp Eliminase KE07 - Crystal 18 Design Trp50Ala mutantDirected evolutionary changes in Kemp Eliminase KE07 - Crystal 18 Design Trp50Ala mutant
Structural highlights
Publication Abstract from PubMedDevelopments in computational chemistry, bioinformatics, and laboratory evolution have facilitated the de novo design and catalytic optimization of enzymes. Besides creating useful catalysts, the generation and iterative improvement of designed enzymes can provide valuable insight into the interplay between the many phenomena that have been suggested to contribute to catalysis. In this work, we follow changes in conformational sampling, electrostatic preorganization, and quantum tunneling along the evolutionary trajectory of a designed Kemp eliminase. We observe that in the Kemp Eliminase KE07, instability of the designed active site leads to the emergence of two additional active site configurations. Evolutionary conformational selection then gradually stabilizes the most efficient configuration, leading to an improved enzyme. This work exemplifies the link between conformational plasticity and evolvability and demonstrates that residues remote from the active sites of enzymes play crucial roles in controlling and shaping the active site for efficient catalysis. The evolution of multiple active site configurations in a designed enzyme.,Hong NS, Petrovic D, Lee R, Gryn'ova G, Purg M, Saunders J, Bauer P, Carr PD, Lin CY, Mabbitt PD, Zhang W, Altamore T, Easton C, Coote ML, Kamerlin SCL, Jackson CJ Nat Commun. 2018 Sep 25;9(1):3900. doi: 10.1038/s41467-018-06305-y. PMID:30254369[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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