7o1d

<table><tr><td colspan='2'>[[7o1d]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7O1D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7O1D FirstGlance]. <br>

</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=7o1d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7o1d OCA], [https://pdbe.org/7o1d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7o1d RCSB], [https://www.ebi.ac.uk/pdbsum/7o1d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7o1d ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

The combination of computational design and directed evolution could offer a general strategy to create enzymes with new functions. So far, this approach has delivered enzymes for a handful of model reactions. Here we show that new catalytic mechanisms can be engineered into proteins to accelerate more challenging chemical transformations. Evolutionary optimization of a primitive design afforded an efficient and enantioselective enzyme (BH32.14) for the Morita-Baylis-Hillman (MBH) reaction. BH32.14 is suitable for preparative-scale transformations, accepts a broad range of aldehyde and enone coupling partners and is able to promote selective monofunctionalizations of dialdehydes. Crystallographic, biochemical and computational studies reveal that BH32.14 operates via a sophisticated catalytic mechanism comprising a His23 nucleophile paired with a judiciously positioned Arg124. This catalytic arginine shuttles between conformational states to stabilize multiple oxyanion intermediates and serves as a genetically encoded surrogate of privileged bidentate hydrogen-bonding catalysts (for example, thioureas). This study demonstrates that elaborate catalytic devices can be built from scratch to promote demanding multi-step processes not observed in nature.

Engineering an efficient and enantioselective enzyme for the Morita-Baylis-Hillman reaction.,Crawshaw R, Crossley AE, Johannissen L, Burke AJ, Hay S, Levy C, Baker D, Lovelock SL, Green AP Nat Chem. 2021 Dec 16. pii: 10.1038/s41557-021-00833-9. doi:, 10.1038/s41557-021-00833-9. PMID:34916595<ref>PMID:34916595</ref>

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

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== References ==

<references/>

[[Category: Levy, C W]]

[[Category: Biosynthetic protein]]

[[Category: De novo enzyme]]