6f97: Difference between revisions
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<StructureSection load='6f97' size='340' side='right' caption='[[6f97]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='6f97' size='340' side='right' caption='[[6f97]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6f97]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6F97 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6F97 FirstGlance]. <br> | <table><tr><td colspan='2'>[[6f97]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mets6 Mets6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6F97 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6F97 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MPQ_0130 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=887061 METS6])</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=6f97 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6f97 OCA], [http://pdbe.org/6f97 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6f97 RCSB], [http://www.ebi.ac.uk/pdbsum/6f97 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6f97 ProSAT]</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=6f97 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6f97 OCA], [http://pdbe.org/6f97 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6f97 RCSB], [http://www.ebi.ac.uk/pdbsum/6f97 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6f97 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Mets6]] | |||
[[Category: Binda, C]] | [[Category: Binda, C]] | ||
[[Category: Faber, K]] | [[Category: Faber, K]] | ||
Latest revision as of 10:20, 28 February 2018
Crystal structure of the V465T mutant of 5-(Hydroxymethyl)furfural Oxidase (HMFO)Crystal structure of the V465T mutant of 5-(Hydroxymethyl)furfural Oxidase (HMFO)
Structural highlights
Function[HMFO_METS6] Involved in the degradation and detoxification of 5-(hydroxymethyl)furfural (HMF) by mediating its oxidation to furan-2,5-dicarboxylate (FDCA), a biobased platform chemical for the production of polymers. Active with a wide range of aromatic and aliphatic primary alcohols and aldehydes: acts on alcohol groups and requires the spontaneous hydration of aldehyde groups for their oxidation (PubMed:24271187, PubMed:24802551). To a lesser extent, is also able to catalyze the oxidation of thiols that are structurally similar to its alcohol substrates, yielding the corresponding thiocarbonyls (PubMed:25284255).[1] [2] [3] Publication Abstract from PubMedVarious flavoprotein oxidases were recently shown to oxidize prim-thiols. Here we extend this reactivity towards sec-thiols via structure-guided engineering of 5-(hydroxymethyl)furfural oxidase (HMFO). The variants obtained were employed for the oxidative kinetic resolution of rac-sec-thiols yielding the correspon notding thioketones and nonreacted (R)-thiols with excellent enantioselectivities (E >/= 200). The engineering strategy applied went beyond the classic approach of replacing bulky amino acid residues with smaller ones, as the active site was additionally enlarged by a newly introduced Thr residue that establishes a hydrogen bonding interaction with the substrates, as predicted by modelling and verified in the crystal structure of the variant. These strategies unlocked HMFO variants for the enantioselective oxidation of a range of sec-thiols. Kinetic Resolution of sec-Thiols via Enantioselective Oxidation with Rationally Engineered 5-(Hydroxymethyl)furfural Oxidase.,Pickl M, Swoboda A, Romero E, Winkler C, Binda C, Mattevi A, Faber K, Fraaije M Angew Chem Int Ed Engl. 2018 Jan 31. doi: 10.1002/anie.201713189. PMID:29384246[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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