1tzl

<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://proteopedia.org/fgij/fg.htm?mol=1TZL FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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 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://proteopedia.org/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], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1tzl ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/P2OX_PENSG 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).

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== 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<ref>PMID:15362852</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Pensg]]

[[Category: Pyranose oxidase]]

[[Category: Bannwarth, M]]

[[Category: Bastian, S]]

[[Category: Giffhorn, F]]

[[Category: Heckmann-Pohl, D]]

[[Category: Schulz, G E]]

[[Category: Oxidoreductase]]