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1tzl

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Revision as of 19:20, 10 September 2015

Crystal Structure of Pyranose 2-Oxidase from the White-Rot Fungus Peniophora sp.

Structural highlights

1tzl is a 8 chain structure with sequence from Pensg. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
NonStd Res:
Gene:	p2ox (PENSG)
Activity:	Pyranose oxidase, with EC number 1.1.3.10
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[P2OX_PENSG] Catalyzes the oxidation of various aldopyranoses and disaccharides on carbon-2 to the corresponding 2-keto sugars concomitant with the reduction of O(2) to H(2)O(2). Plays an important role in lignin degradation of wood rot fungi by supplying the essential cosubstrate H(2)O(2) for the ligninolytic peroxidases, lignin peroxidase and manganese-dependent peroxidase (By similarity).

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

Pyranose 2-oxidase catalyzes the oxidation of a number of carbohydrates using dioxygen. The enzyme forms a D(2) symmetric homotetramer and contains one covalently bound FAD per subunit. The structure of the enzyme from Peniophora sp. was determined by multiwavelength anomalous diffraction (MAD) based on 96 selenium sites per crystallographic asymmetric unit and subsequently refined to good-quality indices. According to its chain fold, the enzyme belongs to the large glutathione reductase family and, in a more narrow sense, to the glucose-methanol-choline oxidoreductase (GMC) family. The tetramer contains a spacious central cavity from which the substrate enters one of the four active centers by penetrating a mobile barrier. Since this cavity can only be accessed by glucose-sized molecules, the enzyme does not convert sugars that are part of a larger molecule. The geometry of the active center and a comparison with an inhibitor complex of the homologous enzyme cellobiose dehydrogenase allow the modeling of the reaction at a high confidence level.

Crystal structure of pyranose 2-oxidase from the white-rot fungus Peniophora sp.,Bannwarth M, Bastian S, Heckmann-Pohl D, Giffhorn F, Schulz GE Biochemistry. 2004 Sep 21;43(37):11683-90. PMID:15362852^[1]

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

References

↑ Bannwarth M, Bastian S, Heckmann-Pohl D, Giffhorn F, Schulz GE. Crystal structure of pyranose 2-oxidase from the white-rot fungus Peniophora sp. Biochemistry. 2004 Sep 21;43(37):11683-90. PMID:15362852 doi:10.1021/bi048609q

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/1tzl"

@@ Line 2: / Line 2: @@
 <StructureSection load='1tzl' size='340' side='right' caption='[[1tzl]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1tzl]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Peniophora_sp._sg Peniophora sp. sg]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TZL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1TZL FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1tzl]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Pensg Pensg]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TZL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1TZL 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></td></tr>
 <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">p2ox ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=204723 Peniophora sp. SG])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">p2ox ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=204723 PENSG])</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pyranose_oxidase Pyranose oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.3.10 1.1.3.10] </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=1tzl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tzl OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1tzl RCSB], [http://www.ebi.ac.uk/pdbsum/1tzl 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=1tzl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tzl OCA], [http://pdbe.org/1tzl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1tzl RCSB], [http://www.ebi.ac.uk/pdbsum/1tzl PDBsum]</span></td></tr>
 </table>
 == Function ==
@@ Line 29: / Line 29: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1tzl" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Pyranose oxidase|Pyranose oxidase]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Peniophora sp. sg]]
+[[Category: Pensg]]
 [[Category: Pyranose oxidase]]
 [[Category: Bannwarth, M]]

1tzl

From Proteopedia

Revision as of 19:20, 10 September 2015

Crystal Structure of Pyranose 2-Oxidase from the White-Rot Fungus Peniophora sp.

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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