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1tzl

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[[Image:1tzl.jpg|left|200px]]<br /><applet load="1tzl" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1tzl, resolution 2.35&Aring;" />
 
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'''Crystal Structure of Pyranose 2-Oxidase from the White-Rot Fungus Peniophora sp.'''<br />
 
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==Overview==
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==Crystal Structure of Pyranose 2-Oxidase from the White-Rot Fungus Peniophora sp.==
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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.
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<StructureSection load='1tzl' size='340' side='right'caption='[[1tzl]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1tzl]] is a 8 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=1TZL FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.35&#8491;</td></tr>
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<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>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1tzl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tzl OCA], [https://pdbe.org/1tzl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tzl RCSB], [https://www.ebi.ac.uk/pdbsum/1tzl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tzl ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://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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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/tz/1tzl_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1tzl ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1TZL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Peniophora_sp._sg Peniophora sp. sg] with <scene name='pdbligand=FAD:'>FAD</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TZL OCA].
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*[[Pyranose oxidase|Pyranose oxidase]]
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__TOC__
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==Reference==
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</StructureSection>
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15362852 15362852]
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[[Category: Large Structures]]
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[[Category: Peniophora sp. sg]]
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[[Category: Peniophora sp. SG]]
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[[Category: Pyranose oxidase]]
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[[Category: Bannwarth M]]
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[[Category: Single protein]]
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[[Category: Bastian S]]
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[[Category: Bannwarth, M.]]
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[[Category: Giffhorn F]]
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[[Category: Bastian, S.]]
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[[Category: Heckmann-Pohl D]]
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[[Category: Giffhorn, F.]]
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[[Category: Schulz GE]]
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[[Category: Heckmann-Pohl, D.]]
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[[Category: Schulz, G E.]]
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[[Category: FAD]]
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[[Category: glucose-methanol-choline family]]
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[[Category: gmc oxidoreductase]]
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[[Category: large inner cavity]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:19:02 2008''
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Current revision

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

PDB ID 1tzl

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