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1e8g
From Proteopedia
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| - | [[Image:1e8g.gif|left|200px]] | + | [[Image:1e8g.gif|left|200px]] |
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| - | '''STRUCTURE OF THE H61T DOUBLE MUTANT OF VANILLYL-ALCOHOL OXIDASE IN COMPLEX WITH FLUORO-CRESOL''' | + | {{Structure |
| + | |PDB= 1e8g |SIZE=350|CAPTION= <scene name='initialview01'>1e8g</scene>, resolution 2.10Å | ||
| + | |SITE= <scene name='pdbsite=AC1:Fad+Binding+Site+For+Chain+A'>AC1</scene>, <scene name='pdbsite=AC2:Fcr+Binding+Site+For+Chain+A'>AC2</scene>, <scene name='pdbsite=AC3:Fad+Binding+Site+For+Chain+B'>AC3</scene> and <scene name='pdbsite=AC4:Fcr+Binding+Site+For+Chain+B'>AC4</scene> | ||
| + | |LIGAND= <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene> and <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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''STRUCTURE OF THE H61T DOUBLE MUTANT OF VANILLYL-ALCOHOL OXIDASE IN COMPLEX WITH FLUORO-CRESOL''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1E8G is a [ | + | 1E8G is a [[Single protein]] structure of 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=1E8G OCA]. |
==Reference== | ==Reference== | ||
| - | Structural analysis of flavinylation in vanillyl-alcohol oxidase., Fraaije MW, van Den Heuvel RH, van Berkel WJ, Mattevi A, J Biol Chem. 2000 Dec 8;275(49):38654-8. PMID:[http:// | + | Structural analysis of flavinylation in vanillyl-alcohol oxidase., Fraaije MW, van Den Heuvel RH, van Berkel WJ, Mattevi A, J Biol Chem. 2000 Dec 8;275(49):38654-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10984479 10984479] |
[[Category: Penicillium simplicissimum]] | [[Category: Penicillium simplicissimum]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: specificity]] | [[Category: specificity]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:51:38 2008'' |
Revision as of 08:51, 20 March 2008
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| , resolution 2.10Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , , and | ||||||
| Ligands: | and | ||||||
| Activity: | Vanillyl-alcohol oxidase, with EC number 1.1.3.38 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF THE H61T DOUBLE MUTANT OF VANILLYL-ALCOHOL OXIDASE IN COMPLEX WITH FLUORO-CRESOL
Overview
Vanillyl-alcohol oxidase (VAO) is member of a newly recognized flavoprotein family of structurally related oxidoreductases. The enzyme contains a covalently linked FAD cofactor. To study the mechanism of flavinylation we have created a design point mutation (His-61 --> Thr). In the mutant enzyme the covalent His-C8alpha-flavin linkage is not formed, while the enzyme is still able to bind FAD and perform catalysis. The H61T mutant displays a similar affinity for FAD and ADP (K(d) = 1.8 and 2.1 microm, respectively) but does not interact with FMN. H61T is about 10-fold less active with 4-(methoxymethyl)phenol) (k(cat) = 0.24 s(-)(1), K(m) = 40 microm) than the wild-type enzyme. The crystal structures of both the holo and apo form of H61T are highly similar to the structure of wild-type VAO, indicating that binding of FAD to the apoprotein does not require major structural rearrangements. These results show that covalent flavinylation is an autocatalytical process in which His-61 plays a crucial role by activating His-422. Furthermore, our studies clearly demonstrate that in VAO, the FAD binds via a typical lock-and-key approach to a preorganized binding site.
About this Structure
1E8G is a Single protein structure of sequence from Penicillium simplicissimum. Full crystallographic information is available from OCA.
Reference
Structural analysis of flavinylation in vanillyl-alcohol oxidase., Fraaije MW, van Den Heuvel RH, van Berkel WJ, Mattevi A, J Biol Chem. 2000 Dec 8;275(49):38654-8. PMID:10984479
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