4bs0

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<StructureSection load='4bs0' size='340' side='right'caption='[[4bs0]], [[Resolution|resolution]] 1.09&Aring;' scene=''>
<StructureSection load='4bs0' size='340' side='right'caption='[[4bs0]], [[Resolution|resolution]] 1.09&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4bs0]] is a 2 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=4BS0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4BS0 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4bs0]] 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=4BS0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BS0 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=6NT:6-NITROBENZOTRIAZOLE'>6NT</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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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=6NT:6-NITROBENZOTRIAZOLE'>6NT</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<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=4bs0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bs0 OCA], [http://pdbe.org/4bs0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4bs0 RCSB], [http://www.ebi.ac.uk/pdbsum/4bs0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4bs0 ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4bs0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bs0 OCA], [https://pdbe.org/4bs0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bs0 RCSB], [https://www.ebi.ac.uk/pdbsum/4bs0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bs0 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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Linus Pauling established the conceptual framework for understanding and mimicking enzymes more than six decades ago. The notion that enzymes selectively stabilize the rate-limiting transition state of the catalysed reaction relative to the bound ground state reduces the problem of design to one of molecular recognition. Nevertheless, past attempts to capitalize on this idea, for example by using transition state analogues to elicit antibodies with catalytic activities, have generally failed to deliver true enzymatic rates. The advent of computational design approaches, combined with directed evolution, has provided an opportunity to revisit this problem. Starting from a computationally designed catalyst for the Kemp elimination-a well-studied model system for proton transfer from carbon-we show that an artificial enzyme can be evolved that accelerates an elementary chemical reaction 6 x 108-fold, approaching the exceptional efficiency of highly optimized natural enzymes such as triosephosphate isomerase. A 1.09 A resolution crystal structure of the evolved enzyme indicates that familiar catalytic strategies such as shape complementarity and precisely placed catalytic groups can be successfully harnessed to afford such high rate accelerations, making us optimistic about the prospects of designing more sophisticated catalysts.
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Precision is essential for efficient catalysis in an evolved Kemp eliminase.,Blomberg R, Kries H, Pinkas DM, Mittl PR, Grutter MG, Privett HK, Mayo SL, Hilvert D Nature. 2013 Oct 16. doi: 10.1038/nature12623. PMID:24132235<ref>PMID:24132235</ref>
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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 4bs0" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Kemp eliminase|Kemp eliminase]]
*[[Kemp eliminase|Kemp eliminase]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Theau]]
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[[Category: Thermoascus aurantiacus]]
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[[Category: Blomberg, R]]
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[[Category: Blomberg R]]
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[[Category: Gruetter, M G]]
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[[Category: Gruetter MG]]
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[[Category: Hilvert, D]]
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[[Category: Hilvert D]]
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[[Category: Kries, H]]
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[[Category: Kries H]]
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[[Category: Mayo, S]]
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[[Category: Mayo S]]
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[[Category: Mittl, P R.E]]
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[[Category: Mittl PRE]]
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[[Category: Pinkas, D M]]
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[[Category: Pinkas DM]]
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[[Category: Privett, H K]]
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[[Category: Privett HK]]
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[[Category: Bottom-up enzyme construction]]
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[[Category: Computational protein design]]
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[[Category: Directed evolution]]
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[[Category: Elementary chemical step catalysis]]
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[[Category: Kemp elimination]]
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[[Category: Lyase-lyase inhibitor complex]]
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[[Category: Proton transfer]]
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[[Category: Transition state tuning]]
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Revision as of 17:03, 7 September 2022

Crystal Structure of Kemp Eliminase HG3.17 E47N,N300D Complexed with Transition State Analog 6-Nitrobenzotriazole

PDB ID 4bs0

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