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5rg6

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Current revision (13:47, 1 March 2024) (edit) (undo)
 
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<StructureSection load='5rg6' size='340' side='right'caption='[[5rg6]], [[Resolution|resolution]] 1.35&Aring;' scene=''>
<StructureSection load='5rg6' size='340' side='right'caption='[[5rg6]], [[Resolution|resolution]] 1.35&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5rg6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Theau Theau]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5RG6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5RG6 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5rg6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermoascus_aurantiacus Thermoascus aurantiacus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5RG6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5RG6 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.35&#8491;</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Endo-1,4-beta-xylanase Endo-1,4-beta-xylanase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.8 3.2.1.8] </span></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=5rg6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5rg6 OCA], [https://pdbe.org/5rg6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5rg6 RCSB], [https://www.ebi.ac.uk/pdbsum/5rg6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5rg6 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=5rg6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5rg6 OCA], [https://pdbe.org/5rg6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5rg6 RCSB], [https://www.ebi.ac.uk/pdbsum/5rg6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5rg6 ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/XYNA_THEAU XYNA_THEAU]
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The creation of artificial enzymes is a key objective of computational protein design. Although de novo enzymes have been successfully designed, these exhibit low catalytic efficiencies, requiring directed evolution to improve activity. Here, we use room-temperature X-ray crystallography to study changes in the conformational ensemble during evolution of the designed Kemp eliminase HG3 (kcat/KM 146 M(-1)s(-1)). We observe that catalytic residues are increasingly rigidified, the active site becomes better pre-organized, and its entrance is widened. Based on these observations, we engineer HG4, an efficient biocatalyst (kcat/KM 103,000 M(-1)s(-1)) containing key first and second-shell mutations found during evolution. HG4 structures reveal that its active site is pre-organized and rigidified for efficient catalysis. Our results show how directed evolution circumvents challenges inherent to enzyme design by shifting conformational ensembles to favor catalytically-productive sub-states, and suggest improvements to the design methodology that incorporate ensemble modeling of crystallographic data.
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Ensemble-based enzyme design can recapitulate the effects of laboratory directed evolution in silico.,Broom A, Rakotoharisoa RV, Thompson MC, Zarifi N, Nguyen E, Mukhametzhanov N, Liu L, Fraser JS, Chica RA Nat Commun. 2020 Sep 23;11(1):4808. doi: 10.1038/s41467-020-18619-x. PMID:32968058<ref>PMID:32968058</ref>
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==See Also==
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*[[Kemp eliminase|Kemp eliminase]]
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5rg6" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Endo-1,4-beta-xylanase]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Theau]]
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[[Category: Thermoascus aurantiacus]]
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[[Category: Broom, A]]
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[[Category: Broom A]]
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[[Category: Chica, R A]]
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[[Category: Chica RA]]
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[[Category: Fraser, J S]]
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[[Category: Fraser JS]]
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[[Category: Rakotoharisoa, R V]]
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[[Category: Rakotoharisoa RV]]
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[[Category: Thompson, M C]]
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[[Category: Thompson MC]]
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[[Category: Hydrolase]]
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Current revision

Crystal Structure of Kemp Eliminase HG3.7 in unbound state, 277K

PDB ID 5rg6

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