8ah9
From Proteopedia
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- | '''Unreleased structure''' | ||
- | + | ==De novo retro-aldolase RAbetaB-16.1== | |
+ | <StructureSection load='8ah9' size='340' side='right'caption='[[8ah9]], [[Resolution|resolution]] 1.75Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[8ah9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8AH9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8AH9 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]] 1.747Å</td></tr> | ||
+ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BEZ:BENZOIC+ACID'>BEZ</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=8ah9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ah9 OCA], [https://pdbe.org/8ah9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ah9 RCSB], [https://www.ebi.ac.uk/pdbsum/8ah9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ah9 ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | While native scaffolds offer a large diversity of shapes and topologies for enzyme engineering, their often unpredictable behavior in response to sequence modification makes de novo generated scaffolds an exciting alternative. Here we explore the customization of the backbone and sequence of a de novo designed eight stranded beta-barrel protein to create catalysts for a retro-aldolase model reaction. We show that active and specific catalysts can be designed in this fold and use directed evolution to further optimize activity and stereoselectivity. Our results support previous suggestions that different folds have different inherent amenability to evolution and this property could account, in part, for the distribution of natural enzymes among different folds. | ||
- | + | Design and optimization of enzymatic activity in a de novo beta-barrel scaffold.,Kipnis Y, Chaib AO, Vorobieva AA, Cai G, Reggiano G, Basanta B, Kumar E, Mittl PRE, Hilvert D, Baker D Protein Sci. 2022 Nov;31(11):e4405. doi: 10.1002/pro.4405. PMID:36305767<ref>PMID:36305767</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | [[Category: | + | </div> |
- | [[Category: | + | <div class="pdbe-citations 8ah9" style="background-color:#fffaf0;"></div> |
- | [[Category: | + | == References == |
- | [[Category: Mittl | + | <references/> |
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Large Structures]] | ||
+ | [[Category: Synthetic construct]] | ||
+ | [[Category: Hilvert D]] | ||
+ | [[Category: Mittl P]] | ||
+ | [[Category: Oualb Chaib A]] |
Current revision
De novo retro-aldolase RAbetaB-16.1
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