View source for 3zof


==Crystal structure of FMN-binding protein (YP_005476) from Thermus thermophilus with bound benzene-1,4-diol==
<StructureSection load='3zof' size='340' side='right'caption='[[3zof]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3zof]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thet2 Thet2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZOF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZOF FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=HQE:BENZENE-1,4-DIOL'>HQE</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3zoc|3zoc]], [[3zod|3zod]], [[3zoe|3zoe]]</div></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=3zof FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zof OCA], [https://pdbe.org/3zof PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zof RCSB], [https://www.ebi.ac.uk/pdbsum/3zof PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zof ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The exploitation of catalytic promiscuity and the application of de novo design have recently opened the access to novel, non-natural enzymatic activities. Here we describe a structural bioinformatic method for predicting catalytic activities of enzymes based on three-dimensional constellations of functional groups in active sites ('catalophores'). As a proof-of-concept we identify two enzymes with predicted promiscuous ene-reductase activity (reduction of activated C-C double bonds) and compare them with known ene-reductases, that is, members of the Old Yellow Enzyme family. Despite completely different amino acid sequences, overall structures and protein folds, high-resolution crystal structures reveal equivalent binding modes of typical Old Yellow Enzyme substrates and ligands. Biochemical and biocatalytic data show that the two enzymes indeed possess ene-reductase activity and reveal an inverted stereopreference compared with Old Yellow Enzymes for some substrates. This method could thus be a tool for the identification of viable starting points for the development and engineering of novel biocatalysts.

Identification of promiscuous ene-reductase activity by mining structural databases using active site constellations.,Steinkellner G, Gruber CC, Pavkov-Keller T, Binter A, Steiner K, Winkler C, Lyskowski A, Schwamberger O, Oberer M, Schwab H, Faber K, Macheroux P, Gruber K Nat Commun. 2014 Jun 23;5:4150. doi: 10.1038/ncomms5150. PMID:24954722<ref>PMID:24954722</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3zof" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Thet2]]
[[Category: Faber, K]]
[[Category: Gruber, C C]]
[[Category: Gruber, K]]
[[Category: Pavkov-Keller, T]]
[[Category: Schwab, H]]
[[Category: Schwamberger, O]]
[[Category: Steiner, K]]
[[Category: Steinkellner, G]]
[[Category: Winkler, C]]
[[Category: Fmn-binding protein]]