1tzl

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(New page: 200px<br /><applet load="1tzl" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tzl, resolution 2.35&Aring;" /> '''Crystal Structure of...)
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[[Image:1tzl.jpg|left|200px]]<br /><applet load="1tzl" size="450" 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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== 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/initialview03.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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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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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==About this Structure==
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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:15362852<ref>PMID:15362852</ref>
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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 FAD 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1TZL OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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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</div>
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[[Category: Peniophora sp. sg]]
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<div class="pdbe-citations 1tzl" style="background-color:#fffaf0;"></div>
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[[Category: Pyranose oxidase]]
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[[Category: Single protein]]
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[[Category: Bannwarth, M.]]
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[[Category: Bastian, S.]]
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[[Category: Giffhorn, F.]]
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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://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 03:43:31 2007''
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==See Also==
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*[[Pyranose oxidase|Pyranose oxidase]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Peniophora sp. SG]]
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[[Category: Bannwarth M]]
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[[Category: Bastian S]]
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[[Category: Giffhorn F]]
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[[Category: Heckmann-Pohl D]]
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[[Category: Schulz GE]]

Current revision

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

PDB ID 1tzl

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