1e0y: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1e0y]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Penicillium_simplicissimum Penicillium simplicissimum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E0Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1E0Y FirstGlance]. <br> | <table><tr><td colspan='2'>[[1e0y]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Penicillium_simplicissimum Penicillium simplicissimum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E0Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1E0Y FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FCR:ALPHA,ALPHA,ALPHA-TRIFLUORO-P-CRESOL'>FCR</scene>< | </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>, <scene name='pdbligand=FCR:ALPHA,ALPHA,ALPHA-TRIFLUORO-P-CRESOL'>FCR</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1vao|1vao]], [[1ahu|1ahu]], [[1ahv|1ahv]], [[1ahz|1ahz]], [[2vao|2vao]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1vao|1vao]], [[1ahu|1ahu]], [[1ahv|1ahv]], [[1ahz|1ahz]], [[2vao|2vao]]</td></tr> | ||
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Vanillyl-alcohol_oxidase Vanillyl-alcohol oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.3.38 1.1.3.38] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Vanillyl-alcohol_oxidase Vanillyl-alcohol oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.3.38 1.1.3.38] </span></td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1e0y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e0y OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1e0y RCSB], [http://www.ebi.ac.uk/pdbsum/1e0y 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=1e0y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e0y OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1e0y RCSB], [http://www.ebi.ac.uk/pdbsum/1e0y PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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[[Category: Penicillium simplicissimum]] | [[Category: Penicillium simplicissimum]] | ||
[[Category: Vanillyl-alcohol oxidase]] | [[Category: Vanillyl-alcohol oxidase]] | ||
[[Category: Berkel, W J.H Van | [[Category: Berkel, W J.H Van]] | ||
[[Category: Heuvel, R H.H Van Der | [[Category: Heuvel, R H.H Van Der]] | ||
[[Category: Mattevi, A | [[Category: Mattevi, A]] | ||
[[Category: Flavoenzyme]] | [[Category: Flavoenzyme]] | ||
[[Category: Specificity]] | [[Category: Specificity]] | ||
Revision as of 03:14, 23 December 2014
STRUCTURE OF THE D170S/T457E DOUBLE MUTANT OF VANILLYL-ALCOHOL OXIDASESTRUCTURE OF THE D170S/T457E DOUBLE MUTANT OF VANILLYL-ALCOHOL OXIDASE
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedVanillyl-alcohol oxidase (VAO) is the prototype of a newly recognized family of structurally related oxidoreductases sharing a conserved FAD-binding domain. The active site of VAO is formed by a cavity where the enzyme is able to catalyze many reactions with phenolic substrates. Among these reactions is the stereospecific hydroxylation of 4-ethylphenol-forming (R)-1-(4'-hydroxyphenyl)ethanol. During this conversion, Asp-170 is probably critical for the hydration of the initially formed p-quinone methide intermediate. By site-directed mutagenesis, the putative active site base has been relocated to the opposite face of the active site cavity. In this way, a change in stereospecificity has been achieved. Like native VAO, the single mutants T457E, D170A, and D170S preferentially converted 4-ethylphenol to the (R)-enantiomer of 1-(4'-hydroxyphenyl)ethanol. The double mutants D170A/T457E and D170S/T457E exhibited an inverted stereospecificity with 4-ethylphenol. Particularly, D170S/T457E was strongly (S)-selective, with an enantiomeric excess of 80%. The crystal structure of D170S/T457E, in complex with trifluoromethylphenol, showed a highly conserved mode of ligand binding and revealed that the distinctive catalytic properties of this mutant are not caused by major structural changes. Inversion of stereospecificity of vanillyl-alcohol oxidase.,van Den Heuvel RH, Fraaije MW, Ferrer M, Mattevi A, van Berkel WJ Proc Natl Acad Sci U S A. 2000 Aug 15;97(17):9455-60. PMID:10920192[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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