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| | <StructureSection load='7k4r' size='340' side='right'caption='[[7k4r]], [[Resolution|resolution]] 1.57Å' scene=''> | | <StructureSection load='7k4r' size='340' side='right'caption='[[7k4r]], [[Resolution|resolution]] 1.57Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[7k4r]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Theau Theau]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7K4R OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=7K4R FirstGlance]. <br> | + | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7K4R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7K4R FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">XYNA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5087 THEAU])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.57Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Endo-1,4-beta-xylanase Endo-1,4-beta-xylanase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.8 3.2.1.8] </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=7k4r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7k4r OCA], [https://pdbe.org/7k4r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7k4r RCSB], [https://www.ebi.ac.uk/pdbsum/7k4r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7k4r ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=7k4r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7k4r OCA], [http://pdbe.org/7k4r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=7k4r RCSB], [http://www.ebi.ac.uk/pdbsum/7k4r PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=7k4r ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
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| | </div> | | </div> |
| | <div class="pdbe-citations 7k4r" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 7k4r" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Kemp eliminase|Kemp eliminase]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Endo-1,4-beta-xylanase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Theau]]
| + | [[Category: Bunzel A]] |
| - | [[Category: Bunzel, A]] | + | [[Category: Cohen AE]] |
| - | [[Category: Cohen, A E]] | + | [[Category: Hilvert D]] |
| - | [[Category: Hilvert, D]] | + | [[Category: Kern D]] |
| - | [[Category: Kern, D]] | + | [[Category: Nguyen V]] |
| - | [[Category: Nguyen, V]] | + | [[Category: Otten R]] |
| - | [[Category: Otten, R]] | + | [[Category: Padua RAP]] |
| - | [[Category: Padua, R A.P]] | + | [[Category: Patterson M]] |
| - | [[Category: Patterson, M]] | + | [[Category: Perry SL]] |
| - | [[Category: Perry, S L]] | + | [[Category: Pitsawong W]] |
| - | [[Category: Pitsawong, W]] | + | [[Category: Sui S]] |
| - | [[Category: Sui, S]] | + | |
| - | [[Category: Directed evolution]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Kemp elimination]]
| + | |
| Structural highlights
Publication Abstract from PubMed
The advent of biocatalysts designed computationally and optimized by laboratory evolution provides an opportunity to explore molecular strategies for augmenting catalytic function. Applying a suite of nuclear magnetic resonance, crystallography, and stopped-flow techniques to an enzyme designed for an elementary proton transfer reaction, we show how directed evolution gradually altered the conformational ensemble of the protein scaffold to populate a narrow, highly active conformational ensemble and accelerate this transformation by nearly nine orders of magnitude. Mutations acquired during optimization enabled global conformational changes, including high-energy backbone rearrangements, that cooperatively organized the catalytic base and oxyanion stabilizer, thus perfecting transition-state stabilization. The development of protein catalysts for many chemical transformations could be facilitated by explicitly sampling conformational substates during design and specifically stabilizing productive substates over all unproductive conformations.
How directed evolution reshapes the energy landscape in an enzyme to boost catalysis.,Otten R, Padua RAP, Bunzel HA, Nguyen V, Pitsawong W, Patterson M, Sui S, Perry SL, Cohen AE, Hilvert D, Kern D Science. 2020 Dec 18;370(6523):1442-1446. doi: 10.1126/science.abd3623. Epub 2020, Nov 19. PMID:33214289[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Otten R, Padua RAP, Bunzel HA, Nguyen V, Pitsawong W, Patterson M, Sui S, Perry SL, Cohen AE, Hilvert D, Kern D. How directed evolution reshapes the energy landscape in an enzyme to boost catalysis. Science. 2020 Dec 18;370(6523):1442-1446. doi: 10.1126/science.abd3623. Epub 2020, Nov 19. PMID:33214289 doi:http://dx.doi.org/10.1126/science.abd3623
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