3zoh: Difference between revisions
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==Crystal structure of FMN-binding protein (YP_005476) from Thermus thermophilus with bound 1-Cyclohex-2-enone== | ==Crystal structure of FMN-binding protein (YP_005476) from Thermus thermophilus with bound 1-Cyclohex-2-enone== | ||
<StructureSection load='3zoh' size='340' side='right' caption='[[3zoh]], [[Resolution|resolution]] 1.65Å' scene=''> | <StructureSection load='3zoh' size='340' side='right' caption='[[3zoh]], [[Resolution|resolution]] 1.65Å' scene=''> | ||
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=A2Q:CYCLOHEX-2-EN-1-ONE'>A2Q</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=A2Q:CYCLOHEX-2-EN-1-ONE'>A2Q</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3zoc|3zoc]], [[3zod|3zod]], [[3zoe|3zoe]], [[3zof|3zof]], [[3zog|3zog]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3zoc|3zoc]], [[3zod|3zod]], [[3zoe|3zoe]], [[3zof|3zof]], [[3zog|3zog]]</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=3zoh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zoh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3zoh RCSB], [http://www.ebi.ac.uk/pdbsum/3zoh PDBsum]</span></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=3zoh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zoh OCA], [http://pdbe.org/3zoh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3zoh RCSB], [http://www.ebi.ac.uk/pdbsum/3zoh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3zoh ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 3zoh" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 19:04, 11 August 2016
Crystal structure of FMN-binding protein (YP_005476) from Thermus thermophilus with bound 1-Cyclohex-2-enoneCrystal structure of FMN-binding protein (YP_005476) from Thermus thermophilus with bound 1-Cyclohex-2-enone
Structural highlights
Publication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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