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| [[Image:1tt0.gif|left|200px]]
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| <!-- | | ==Crystal Structure of Pyranose 2-Oxidase== |
| The line below this paragraph, containing "STRUCTURE_1tt0", creates the "Structure Box" on the page.
| | <StructureSection load='1tt0' size='340' side='right'caption='[[1tt0]], [[Resolution|resolution]] 1.80Å' scene=''> |
| You may change the PDB parameter (which sets the PDB file loaded into the applet) | | == Structural highlights == |
| or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
| | <table><tr><td colspan='2'>[[1tt0]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Trametes_ochracea Trametes ochracea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TT0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TT0 FirstGlance]. <br> |
| or leave the SCENE parameter empty for the default display.
| | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> |
| -->
| | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=12P:DODECAETHYLENE+GLYCOL'>12P</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr> |
| {{STRUCTURE_1tt0| PDB=1tt0 | SCENE= }}
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1tt0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tt0 OCA], [https://pdbe.org/1tt0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tt0 RCSB], [https://www.ebi.ac.uk/pdbsum/1tt0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tt0 ProSAT]</span></td></tr> |
| | </table> |
| | == Function == |
| | [https://www.uniprot.org/uniprot/Q7ZA32_TRAOC Q7ZA32_TRAOC] |
| | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] |
| | Check<jmol> |
| | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/tt/1tt0_consurf.spt"</scriptWhenChecked> |
| | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> |
| | </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=1tt0 ConSurf]. |
| | <div style="clear:both"></div> |
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| '''Crystal Structure of Pyranose 2-Oxidase'''
| | ==See Also== |
| | | *[[Pyranose oxidase|Pyranose oxidase]] |
| | | __TOC__ |
| ==Overview== | | </StructureSection> |
| Pyranose 2-oxidase (P2Ox) is a 270 kDa homotetramer localized preferentially in the hyphal periplasmic space of lignocellulolytic fungi and has a proposed role in lignocellulose degradation to produce the essential co-substrate, hydrogen peroxide, for lignin peroxidases. P2Ox oxidizes D-glucose and other aldopyranoses regioselectively at C2 to the corresponding 2-keto sugars; however, for some substrates, the enzyme also displays specificity for oxidation at C3. The crystal structure of P2Ox from Trametes multicolor has been determined using single anomalous dispersion with mercury as anomalous scatterer. The model was refined at 1.8A resolution to R and Rfree values of 0.134 and 0.171, respectively. The overall fold of the P2Ox subunit resembles that of members of the glucose-methanol-choline family of long-chain oxidoreductases, featuring a flavin-binding Rossmann domain of class alpha/beta and a substrate-binding subdomain with a six-stranded central beta sheet and three alpha helices. The homotetramer buries a large internal cavity of roughly 15,000 A3, from which the four active sites are accessible. Four solvent channels lead from the surface into the cavity through which substrate must enter before accessing the active site. The present structure shows an acetate molecule bound in the active site with the carboxylate group positioned immediately below the flavin N5 atom, and with one carboxylate oxygen atom interacting with the catalytic residues His548 and Asn593. The entrance to the active site is blocked by a loop (residues 452 to 461) with excellent electron density but elevated temperature factors. We predict that this loop is dynamic and opens to allow substrate entry and exit. In silico docking of D-glucose in the P2Ox active site shows that with the active-site loop in the closed conformation, monosaccharides cannot be accommodated; however, after removing the loop from the model, a tentative set of protein-substrate interactions for beta-D-glucose have been outlined. | | [[Category: Large Structures]] |
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| ==About this Structure==
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| 1TT0 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Trametes_ochracea Trametes ochracea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TT0 OCA].
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| ==Reference==
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| Crystal structure of the 270 kDa homotetrameric lignin-degrading enzyme pyranose 2-oxidase., Hallberg BM, Leitner C, Haltrich D, Divne C, J Mol Biol. 2004 Aug 13;341(3):781-96. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15288786 15288786]
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| [[Category: Pyranose oxidase]]
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| [[Category: Single protein]] | |
| [[Category: Trametes ochracea]] | | [[Category: Trametes ochracea]] |
| [[Category: Divne, C.]] | | [[Category: Divne C]] |
| [[Category: Hallberg, B M.]] | | [[Category: Hallberg BM]] |
| [[Category: Haltrich, D.]] | | [[Category: Haltrich D]] |
| [[Category: Leitner, C.]] | | [[Category: Leitner C]] |
| [[Category: Alpha/beta structure]]
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| [[Category: Gmc oxidoreductase]]
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| [[Category: Homotetramer]]
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| [[Category: Phbh fold]]
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| [[Category: Rossman fold]]
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| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 10:19:38 2008''
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