View source for 3u26


==Crystal Structure of Engineered Protein. Northeast Structural Genomics Consortium Target OR48==
<StructureSection load='3u26' size='340' side='right'caption='[[3u26]], [[Resolution|resolution]] 1.59&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3u26]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3U26 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3U26 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.59&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=3u26 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u26 OCA], [https://pdbe.org/3u26 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3u26 RCSB], [https://www.ebi.ac.uk/pdbsum/3u26 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3u26 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/O58216_PYRHO O58216_PYRHO] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The Morita-Baylis-Hillman reaction forms a carbon-carbon bond between the alpha-carbon of a conjugated carbonyl compound and a carbon electrophile. The reaction mechanism involves Michael addition of a nucleophile catalyst at the carbonyl beta-carbon, followed by bond formation with the electrophile and catalyst disassociation to release the product. We used Rosetta to design 48 proteins containing active sites predicted to carry out this mechanism, of which two show catalytic activity by mass spectrometry (MS). Substrate labeling measured by MS and site-directed mutagenesis experiments show that the designed active-site residues are responsible for activity, although rate acceleration over background is modest. To characterize the designed proteins, we developed a fluorescence-based screen for intermediate formation in cell lysates, carried out microsecond molecular dynamics simulations, and solved X-ray crystal structures. These data indicate a partially formed active site and suggest several clear avenues for designing more active catalysts.

Computational design of enone-binding proteins with catalytic activity for the Morita-Baylis-Hillman reaction.,Bjelic S, Nivon LG, Celebi-Olcum N, Kiss G, Rosewall CF, Lovick HM, Ingalls EL, Gallaher JL, Seetharaman J, Lew S, Montelione GT, Hunt JF, Michael FE, Houk KN, Baker D ACS Chem Biol. 2013 Apr 19;8(4):749-57. doi: 10.1021/cb3006227. Epub 2013 Jan 30. PMID:23330600<ref>PMID:23330600</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3u26" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pyrococcus horikoshii]]
[[Category: Acton TB]]
[[Category: Baker D]]
[[Category: Bjelic S]]
[[Category: Ciccosanti C]]
[[Category: Everett JK]]
[[Category: Hunt JF]]
[[Category: Lew S]]
[[Category: Montelione GT]]
[[Category: Nivon L]]
[[Category: Sahdev S]]
[[Category: Seetharaman J]]
[[Category: Tong L]]
[[Category: Xiao R]]