6s97
From Proteopedia
(Difference between revisions)
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<StructureSection load='6s97' size='340' side='right'caption='[[6s97]], [[Resolution|resolution]] 1.95Å' scene=''> | <StructureSection load='6s97' size='340' side='right'caption='[[6s97]], [[Resolution|resolution]] 1.95Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'> | + | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6S97 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6S97 FirstGlance]. <br> |
- | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.953Å</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=6s97 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6s97 OCA], [https://pdbe.org/6s97 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6s97 RCSB], [https://www.ebi.ac.uk/pdbsum/6s97 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6s97 ProSAT]</span></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=6s97 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6s97 OCA], [https://pdbe.org/6s97 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6s97 RCSB], [https://www.ebi.ac.uk/pdbsum/6s97 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6s97 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | Protein dynamics are often invoked in explanations of enzyme catalysis, but their design has proven elusive. Here we track the role of dynamics in evolution, starting from the evolvable and thermostable ancestral protein Anc(HLD-RLuc) which catalyses both dehalogenase and luciferase reactions. Insertion-deletion (InDel) backbone mutagenesis of Anc(HLD-RLuc) challenged the scaffold dynamics. Screening for both activities reveals InDel mutations localized in three distinct regions that lead to altered protein dynamics (based on crystallographic B-factors, hydrogen exchange, and molecular dynamics simulations). An anisotropic network model highlights the importance of the conformational flexibility of a loop-helix fragment of Renilla luciferases for ligand binding. Transplantation of this dynamic fragment leads to lower product inhibition and highly stable glow-type bioluminescence. The success of our approach suggests that a strategy comprising (i) constructing a stable and evolvable template, (ii) mapping functional regions by backbone mutagenesis, and (iii) transplantation of dynamic features, can lead to functionally innovative proteins. | ||
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- | Engineering the protein dynamics of an ancestral luciferase.,Schenkmayerova A, Pinto GP, Toul M, Marek M, Hernychova L, Planas-Iglesias J, Daniel Liskova V, Pluskal D, Vasina M, Emond S, Dorr M, Chaloupkova R, Bednar D, Prokop Z, Hollfelder F, Bornscheuer UT, Damborsky J Nat Commun. 2021 Jun 14;12(1):3616. doi: 10.1038/s41467-021-23450-z. PMID:34127663<ref>PMID:34127663</ref> | ||
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- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
- | </div> | ||
- | <div class="pdbe-citations 6s97" style="background-color:#fffaf0;"></div> | ||
- | == References == | ||
- | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | + | [[Category: Damborsky J]] | |
- | [[Category: Damborsky | + | [[Category: Marek M]] |
- | [[Category: Marek | + | [[Category: Schenkmayerova A]] |
- | [[Category: Schenkmayerova | + | |
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Current revision
Fragment transplantation onto a hyperstable ancestor of haloalkane dehalogenases and Renilla luciferase (Anc-FT)
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