1e8g
From Proteopedia
(New page: 200px<br /> <applet load="1e8g" size="450" color="white" frame="true" align="right" spinBox="true" caption="1e8g, resolution 2.10Å" /> '''STRUCTURE OF THE H6...) |
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==About this Structure== | ==About this Structure== | ||
| - | 1E8G is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Penicillium_simplicissimum Penicillium simplicissimum]] with FAD and FCR as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.3.38 1.1.3.38]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1E8G OCA]]. | + | 1E8G is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Penicillium_simplicissimum Penicillium simplicissimum]] with FAD and FCR as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[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]]. Structure known Active Sites: AC1, AC2, AC3 and AC4. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1E8G OCA]]. |
==Reference== | ==Reference== | ||
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[[Category: Penicillium simplicissimum]] | [[Category: Penicillium simplicissimum]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| + | [[Category: Vanillyl-alcohol oxidase]] | ||
[[Category: Fraaije, M.W.]] | [[Category: Fraaije, M.W.]] | ||
[[Category: Mattevi, A.]] | [[Category: Mattevi, A.]] | ||
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[[Category: specificity]] | [[Category: specificity]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 11:10:47 2007'' |
Revision as of 09:06, 30 October 2007
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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, ... [(full description)]
About this Structure
1E8G is a [Single protein] structure of sequence from [Penicillium simplicissimum] with FAD and FCR as [ligands]. Active as [Vanillyl-alcohol oxidase], with EC number [1.1.3.38]. Structure known Active Sites: AC1, AC2, AC3 and AC4. 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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