1e0y
From Proteopedia
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|PDB= 1e0y |SIZE=350|CAPTION= <scene name='initialview01'>1e0y</scene>, resolution 2.75Å | |PDB= 1e0y |SIZE=350|CAPTION= <scene name='initialview01'>1e0y</scene>, resolution 2.75Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene> | + | |LIGAND= <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FCR:ALPHA,ALPHA,ALPHA-TRIFLUORO-P-CRESOL'>FCR</scene> |
| - | |ACTIVITY= [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] | + | |ACTIVITY= <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> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<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.ebi.ac.uk/pdbsum/1e0y PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1e0y RCSB]</span> | ||
}} | }} | ||
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[[Category: Heuvel, R H.H Van Der.]] | [[Category: Heuvel, R H.H Van Der.]] | ||
[[Category: Mattevi, A.]] | [[Category: Mattevi, A.]] | ||
| - | [[Category: FAD]] | ||
| - | [[Category: FCR]] | ||
[[Category: flavoenzyme]] | [[Category: flavoenzyme]] | ||
[[Category: specificity]] | [[Category: specificity]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:52:47 2008'' |
Revision as of 16:52, 30 March 2008
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| , resolution 2.75Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Activity: | Vanillyl-alcohol oxidase, with EC number 1.1.3.38 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF THE D170S/T457E DOUBLE MUTANT OF VANILLYL-ALCOHOL OXIDASE
Overview
Vanillyl-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.
About this Structure
1E0Y is a Single protein structure of sequence from Penicillium simplicissimum. Full crystallographic information is available from OCA.
Reference
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
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