1e8g

From Proteopedia

(Difference between revisions)

Revision as of 22:08, 9 September 2015

STRUCTURE OF THE H61T DOUBLE MUTANT OF VANILLYL-ALCOHOL OXIDASE IN COMPLEX WITH FLUORO-CRESOL

Structural highlights

1e8g is a 2 chain structure with sequence from Cbs 275.83. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	1e8f, 1e8h, 1ahu, 1ahv, 1ahz, 1dzn, 1e0y, 1qlt, 1qlu, 1vao, 2vao
Activity:	Vanillyl-alcohol oxidase, with EC number 1.1.3.38
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[VAOX_PENSI] Catalyzes the conversion of vanillin alcohol to vanillin, and also the conversion of a wide range of phenolic compounds bearing side chains of variable size at the para position of the aromatic ring. Crucial for the degradation of the secondary metabolites derived from the degradation of the lignin. Catalyzes besides the oxidation of 4-hydroxybenzyl alcohols, the oxidative deamination of 4-hydroxybenzylamines, the oxidative demethylation of 4-(methoxy-methyl)phenols and the oxidative hydration of 4-allylphenols. Most active with 4-allylphenols.

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 PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Fraaije MW, van Den Heuvel RH, van Berkel WJ, Mattevi A. Structural analysis of flavinylation in vanillyl-alcohol oxidase. J Biol Chem. 2000 Dec 8;275(49):38654-8. PMID:10984479 doi:http://dx.doi.org/10.1074/jbc.M004753200

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1e8g"

@@ Line 2: / Line 2: @@
 <StructureSection load='1e8g' size='340' side='right' caption='[[1e8g]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1e8g]] 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=1E8G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1E8G FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1e8g]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Cbs_275.83 Cbs 275.83]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E8G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1E8G 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>, <scene name='pdbligand=FCR:ALPHA,ALPHA,ALPHA-TRIFLUORO-P-CRESOL'>FCR</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1e8f|1e8f]], [[1e8h|1e8h]], [[1ahu|1ahu]], [[1ahv|1ahv]], [[1ahz|1ahz]], [[1dzn|1dzn]], [[1e0y|1e0y]], [[1qlt|1qlt]], [[1qlu|1qlu]], [[1vao|1vao]], [[2vao|2vao]]</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 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=1e8g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e8g OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1e8g RCSB], [http://www.ebi.ac.uk/pdbsum/1e8g 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=1e8g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e8g OCA], [http://pdbe.org/1e8g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1e8g RCSB], [http://www.ebi.ac.uk/pdbsum/1e8g PDBsum]</span></td></tr>
 </table>
 == Function ==
@@ Line 28: / Line 28: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1e8g" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 35: / Line 36: @@
 __TOC__
 </StructureSection>
-[[Category: Penicillium simplicissimum]]
+[[Category: Cbs 275 83]]
 [[Category: Vanillyl-alcohol oxidase]]
 [[Category: Fraaije, M W]]

1e8g

From Proteopedia

Revision as of 22:08, 9 September 2015

STRUCTURE OF THE H61T DOUBLE MUTANT OF VANILLYL-ALCOHOL OXIDASE IN COMPLEX WITH FLUORO-CRESOL

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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