View source for 4bs0

==Crystal Structure of Kemp Eliminase HG3.17 E47N,N300D Complexed with Transition State Analog 6-Nitrobenzotriazole==
<StructureSection load='4bs0' size='340' side='right' caption='[[4bs0]], [[Resolution|resolution]] 1.09&Aring;' scene=''>
== Structural highlights ==
<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>
</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>
<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://www.rcsb.org/pdb/explore.do?structureId=4bs0 RCSB], [http://www.ebi.ac.uk/pdbsum/4bs0 PDBsum]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>

==See Also==
*[[Kemp eliminase|Kemp eliminase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Theau]]
[[Category: Blomberg, R]]
[[Category: Gruetter, M G]]
[[Category: Hilvert, D]]
[[Category: Kries, H]]
[[Category: Mayo, S]]
[[Category: Mittl, P R.E]]
[[Category: Pinkas, D M]]
[[Category: Privett, H K]]
[[Category: Bottom-up enzyme construction]]
[[Category: Computational protein design]]
[[Category: Directed evolution]]
[[Category: Elementary chemical step catalysis]]
[[Category: Kemp elimination]]
[[Category: Lyase-lyase inhibitor complex]]
[[Category: Proton transfer]]
[[Category: Transition state tuning]]