3zoh: Difference between revisions
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The | ==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=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3zoh]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB27 Thermus thermophilus HB27]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZOH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZOH 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]] 1.65Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A2Q:CYCLOHEX-2-EN-1-ONE'>A2Q</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</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=3zoh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zoh OCA], [https://pdbe.org/3zoh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zoh RCSB], [https://www.ebi.ac.uk/pdbsum/3zoh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zoh ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q72HI0_THET2 Q72HI0_THET2] | |||
<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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3zoh" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Thermus thermophilus HB27]] | |||
[[Category: Faber K]] | |||
[[Category: Gruber CC]] | |||
[[Category: Gruber K]] | |||
[[Category: Pavkov-Keller T]] | |||
[[Category: Schwab H]] | |||
[[Category: Schwamberger O]] | |||
[[Category: Steiner K]] | |||
[[Category: Steinkellner G]] | |||
[[Category: Winkler C]] | |||
Latest revision as of 14:08, 20 December 2023
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
FunctionPublication 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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