4mih - Revision history

OCA at 12:26, 1 March 2024

OCA — Fri, 01 Mar 2024 12:26:55 GMT

←Older revision		Revision as of 12:26, 1 March 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4mih]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Phanerodontia_chrysosporium Phanerodontia chrysosporium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MIH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MIH FirstGlance]. <br>		<table><tr><td colspan='2'>[[4mih]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Phanerodontia_chrysosporium Phanerodontia chrysosporium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MIH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MIH 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>, <scene name='pdbligand=G3F:3-DEOXY-3-FLUORO-BETA-D-GLUCOPYRANOSE'>G3F</scene></td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2.4Å</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>, <scene name='pdbligand=G3F:3-DEOXY-3-FLUORO-BETA-D-GLUCOPYRANOSE'>G3F</scene></td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4mih FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mih OCA], [https://pdbe.org/4mih PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4mih RCSB], [https://www.ebi.ac.uk/pdbsum/4mih PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4mih ProSAT]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4mih FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mih OCA], [https://pdbe.org/4mih PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4mih RCSB], [https://www.ebi.ac.uk/pdbsum/4mih PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4mih ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/P2OX_PHACH P2OX_PHACH] 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. The preferred substrate is D-glucose which is converted to 2-dehydro-D-glucose, an intermediate of a secondary metabolic pathway leading to the antibiotic cortalcerone. Acts also on D-xylose, together with D-glucose the major sugars derived from wood, on L-sorbose, D-galactose and 1,5-anhydroglucitol, a diagnostic marker of diabetes mellitus.<ref>PMID:9210340</ref> <ref>PMID:8661938</ref>		[https://www.uniprot.org/uniprot/P2OX_PHACH P2OX_PHACH] 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. The preferred substrate is D-glucose which is converted to 2-dehydro-D-glucose, an intermediate of a secondary metabolic pathway leading to the antibiotic cortalcerone. Acts also on D-xylose, together with D-glucose the major sugars derived from wood, on L-sorbose, D-galactose and 1,5-anhydroglucitol, a diagnostic marker of diabetes mellitus.<ref>PMID:9210340</ref> <ref>PMID:8661938</ref>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	The flavin-dependent homotetrameric enzyme pyranose 2-oxidase (P2O) is found mostly, but not exclusively, in lignocellulose-degrading fungi where it catalyzes the oxidation of beta-d-glucose to the corresponding 2-keto sugar concomitantly with hydrogen peroxide formation during lignin solubilization. Here, we present crystal structures of P2O from the efficient lignocellulolytic basidiomycete Phanerochaete chrysosporium. Structures were determined of wild-type PcP2O from the natural fungal source, and two variants of recombinant full-length PcP2O, both in complex with the slow substrate 3-deoxy-3-fluoro-beta-d-glucose. The active sites in PcP2O and P2O from Trametes multicolor (TmP2O) are highly conserved with identical substrate binding. Our structural analysis suggests that the 17 degrees C higher melting temperature of PcP2O compared to TmP2O is due to an increased number of intersubunit salt bridges. The structure of recombinant PcP2O expressed with its natural N-terminal sequence, including a proposed propeptide segment, reveals that the first five residues of the propeptide intercalate at the interface between A and B subunits to form stabilizing, mainly hydrophobic, interactions. In the structure of mature PcP2O purified from the natural source, the propeptide segment in subunit A has been replaced by a nearby loop in the B subunit. We propose that the propeptide in subunit A stabilizes the A/B interface of essential dimers in the homotetramer and that, upon maturation, it is replaced by the loop in the B subunit to form the mature subunit interface. This would imply that the propeptide segment of PcP2O acts as an intramolecular chaperone for oligomerization at the A/B interface of the essential dimer.
-
-	Crystal structures of pyranose 2-oxidase suggest that the N-terminus acts as a propeptide that assists in homotetramer assembly.,Hassan N, Tan TC, Spadiut O, Pisanelli I, Fusco L, Haltrich D, Peterbauer CK, Divne C FEBS Open Bio. 2013 Nov 5;3:496-504. PMID:24282677<ref>PMID:24282677</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 4mih" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==

OCA at 09:40, 28 December 2022

OCA — Wed, 28 Dec 2022 09:40:11 GMT

←Older revision		Revision as of 09:40, 28 December 2022
Line 1:		Line 1:
-	~~{{Large structure}}~~	+
	==Pyranose 2-oxidase from Phanerochaete chrysosporium, recombinant H158A mutant==		==Pyranose 2-oxidase from Phanerochaete chrysosporium, recombinant H158A mutant==
-	<StructureSection load='4mih' size='340' side='right' caption='[[4mih]], [[Resolution\|resolution]] 2.40Å' scene=''>	+	<StructureSection load='4mih' size='340' side='right'caption='[[4mih]], [[Resolution\|resolution]] 2.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4mih]] is a 8 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Chrysosporium_pruinosum_(gilman_&_abbott)_carmich. Chrysosporium pruinosum (gilman & abbott) carmich.~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MIH OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4MIH FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4mih]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Phanerodontia_chrysosporium Phanerodontia chrysosporium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MIH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MIH 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>, <scene name='pdbligand=G3F:3-DEOXY-3-FLUORO-BETA-D-GLUCOPYRANOSE'>G3F</scene~~></td></tr>~~	+	</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>, <scene name='pdbligand=G3F:3-DEOXY-3-FLUORO-BETA-D-GLUCOPYRANOSE'>G3F</scene></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4mif\|4mif]], [[4mig\|4mig]]</td></tr>~~	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4mih FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mih OCA], [https://pdbe.org/4mih PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4mih RCSB], [https://www.ebi.ac.uk/pdbsum/4mih PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4mih ProSAT]</span></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">p2o, p2ox, pox ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5306 Chrysosporium pruinosum (Gilman & Abbott) Carmich.])</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=4mih FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mih OCA], [~~http~~://pdbe.org/4mih PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4mih RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4mih PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4mih ProSAT]</span></td></tr>	+
	</table>		</table>
-	{{Large structure}}
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/P2OX_PHACH P2OX_PHACH]] 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. The preferred substrate is D-glucose which is converted to 2-dehydro-D-glucose, an intermediate of a secondary metabolic pathway leading to the antibiotic cortalcerone. Acts also on D-xylose, together with D-glucose the major sugars derived from wood, on L-sorbose, D-galactose and 1,5-anhydroglucitol, a diagnostic marker of diabetes mellitus.<ref>PMID:9210340</ref> <ref>PMID:8661938</ref>	+	[https://www.uniprot.org/uniprot/P2OX_PHACH P2OX_PHACH] 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. The preferred substrate is D-glucose which is converted to 2-dehydro-D-glucose, an intermediate of a secondary metabolic pathway leading to the antibiotic cortalcerone. Acts also on D-xylose, together with D-glucose the major sugars derived from wood, on L-sorbose, D-galactose and 1,5-anhydroglucitol, a diagnostic marker of diabetes mellitus.<ref>PMID:9210340</ref> <ref>PMID:8661938</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 22:		Line 18:
	</div>		</div>
	<div class="pdbe-citations 4mih" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4mih" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Pyranose oxidase\|Pyranose oxidase]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Pyranose oxidase~~]]	+	[[Category: Large Structures]]
-	[[Category: Divne, C]]	+	[[Category: Phanerodontia chrysosporium]]
-	[[Category: Fusco, L]]	+	[[Category: Divne C]]
-	[[Category: Haltrich, D]]	+	[[Category: Fusco L]]
-	[[Category: Hassan, N]]	+	[[Category: Haltrich D]]
-	[[Category: Peterbauer, C]]	+	[[Category: Hassan N]]
-	[[Category: Pisanelli, I]]	+	[[Category: Peterbauer C]]
-	[[Category: Spadiut, O]]	+	[[Category: Pisanelli I]]
-	[[Category: Tan~~, T C]]~~	+	[[Category: Spadiut O]]
-	~~[[Category: Flavinylation]]~~	+	[[Category: Tan TC]]
-	~~[[Category: Gmc oxidoreductase]]~~	+
-	~~[[Category: Homotetramer]]~~	+
-	~~[[Category: Hyphae]]~~	+
-	~~[[Category: Oxidoreductase]]~~	+
-	~~[[Category: Phbh fold]]~~	+
-	~~[[Category: Pyranose 2-oxidaser oxidoreductase]]~~	+
-	~~[[Category: Rossmann fold~~]]	+

OCA at 09:52, 15 November 2017

OCA — Wed, 15 Nov 2017 09:52:00 GMT

←Older revision		Revision as of 09:52, 15 November 2017
Line 22:		Line 22:
	</div>		</div>
	<div class="pdbe-citations 4mih" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4mih" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Pyranose oxidase\|Pyranose oxidase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 18:32, 4 August 2016

OCA — Thu, 04 Aug 2016 18:32:06 GMT

←Older revision		Revision as of 18:32, 4 August 2016
Line 1:		Line 1:
		+	{{Large structure}}
	==Pyranose 2-oxidase from Phanerochaete chrysosporium, recombinant H158A mutant==		==Pyranose 2-oxidase from Phanerochaete chrysosporium, recombinant H158A mutant==
	<StructureSection load='4mih' size='340' side='right' caption='[[4mih]], [[Resolution\|resolution]] 2.40Å' scene=''>		<StructureSection load='4mih' size='340' side='right' caption='[[4mih]], [[Resolution\|resolution]] 2.40Å' scene=''>
Line 7:		Line 8:
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">p2o, p2ox, pox ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5306 Chrysosporium pruinosum (Gilman & Abbott) Carmich.])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">p2o, p2ox, pox ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5306 Chrysosporium pruinosum (Gilman & Abbott) Carmich.])</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='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=4mih FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mih OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4mih RCSB], [http://www.ebi.ac.uk/pdbsum/4mih 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=4mih FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mih OCA], [http://pdbe.org/4mih PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4mih RCSB], [http://www.ebi.ac.uk/pdbsum/4mih PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4mih ProSAT]</span></td></tr>
	</table>		</table>
		+	{{Large structure}}
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/P2OX_PHACH P2OX_PHACH]] 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. The preferred substrate is D-glucose which is converted to 2-dehydro-D-glucose, an intermediate of a secondary metabolic pathway leading to the antibiotic cortalcerone. Acts also on D-xylose, together with D-glucose the major sugars derived from wood, on L-sorbose, D-galactose and 1,5-anhydroglucitol, a diagnostic marker of diabetes mellitus.<ref>PMID:9210340</ref> <ref>PMID:8661938</ref>		[[http://www.uniprot.org/uniprot/P2OX_PHACH P2OX_PHACH]] 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. The preferred substrate is D-glucose which is converted to 2-dehydro-D-glucose, an intermediate of a secondary metabolic pathway leading to the antibiotic cortalcerone. Acts also on D-xylose, together with D-glucose the major sugars derived from wood, on L-sorbose, D-galactose and 1,5-anhydroglucitol, a diagnostic marker of diabetes mellitus.<ref>PMID:9210340</ref> <ref>PMID:8661938</ref>
Line 19:		Line 21:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 4mih" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Pyranose oxidase\|Pyranose oxidase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 11:56, 25 December 2014

OCA — Thu, 25 Dec 2014 11:56:26 GMT

←Older revision		Revision as of 11:56, 25 December 2014
Line 1:		Line 1:
-	~~{{Large structure}}~~	+	==Pyranose 2-oxidase from Phanerochaete chrysosporium, recombinant H158A mutant==
-	~~{{STRUCTURE_4mih\| PDB=4mih \| SCENE= }}~~	+	<StructureSection load='4mih' size='340' side='right' caption='[[4mih]], [[Resolution\|resolution]] 2.40Å' scene=''>
-	===Pyranose 2-oxidase from Phanerochaete chrysosporium, recombinant H158A mutant===	+	== Structural highlights ==
-	~~{{ABSTRACT_PUBMED_24282677}}~~	+	<table><tr><td colspan='2'>[[4mih]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Chrysosporium_pruinosum_(gilman_&_abbott)_carmich. Chrysosporium pruinosum (gilman & abbott) carmich.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MIH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4MIH 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>, <scene name='pdbligand=G3F:3-DEOXY-3-FLUORO-BETA-D-GLUCOPYRANOSE'>G3F</scene></td></tr>
-	==Function==	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4mif\|4mif]], [[4mig\|4mig]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">p2o, p2ox, pox ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5306 Chrysosporium pruinosum (Gilman & Abbott) Carmich.])</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=4mih FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mih OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4mih RCSB], [http://www.ebi.ac.uk/pdbsum/4mih PDBsum]</span></td></tr>
		+	</table>
		+	== Function ==
	[[http://www.uniprot.org/uniprot/P2OX_PHACH P2OX_PHACH]] 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. The preferred substrate is D-glucose which is converted to 2-dehydro-D-glucose, an intermediate of a secondary metabolic pathway leading to the antibiotic cortalcerone. Acts also on D-xylose, together with D-glucose the major sugars derived from wood, on L-sorbose, D-galactose and 1,5-anhydroglucitol, a diagnostic marker of diabetes mellitus.<ref>PMID:9210340</ref> <ref>PMID:8661938</ref>		[[http://www.uniprot.org/uniprot/P2OX_PHACH P2OX_PHACH]] 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. The preferred substrate is D-glucose which is converted to 2-dehydro-D-glucose, an intermediate of a secondary metabolic pathway leading to the antibiotic cortalcerone. Acts also on D-xylose, together with D-glucose the major sugars derived from wood, on L-sorbose, D-galactose and 1,5-anhydroglucitol, a diagnostic marker of diabetes mellitus.<ref>PMID:9210340</ref> <ref>PMID:8661938</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The flavin-dependent homotetrameric enzyme pyranose 2-oxidase (P2O) is found mostly, but not exclusively, in lignocellulose-degrading fungi where it catalyzes the oxidation of beta-d-glucose to the corresponding 2-keto sugar concomitantly with hydrogen peroxide formation during lignin solubilization. Here, we present crystal structures of P2O from the efficient lignocellulolytic basidiomycete Phanerochaete chrysosporium. Structures were determined of wild-type PcP2O from the natural fungal source, and two variants of recombinant full-length PcP2O, both in complex with the slow substrate 3-deoxy-3-fluoro-beta-d-glucose. The active sites in PcP2O and P2O from Trametes multicolor (TmP2O) are highly conserved with identical substrate binding. Our structural analysis suggests that the 17 degrees C higher melting temperature of PcP2O compared to TmP2O is due to an increased number of intersubunit salt bridges. The structure of recombinant PcP2O expressed with its natural N-terminal sequence, including a proposed propeptide segment, reveals that the first five residues of the propeptide intercalate at the interface between A and B subunits to form stabilizing, mainly hydrophobic, interactions. In the structure of mature PcP2O purified from the natural source, the propeptide segment in subunit A has been replaced by a nearby loop in the B subunit. We propose that the propeptide in subunit A stabilizes the A/B interface of essential dimers in the homotetramer and that, upon maturation, it is replaced by the loop in the B subunit to form the mature subunit interface. This would imply that the propeptide segment of PcP2O acts as an intramolecular chaperone for oligomerization at the A/B interface of the essential dimer.

-	~~==About this Structure==~~	+	Crystal structures of pyranose 2-oxidase suggest that the N-terminus acts as a propeptide that assists in homotetramer assembly.,Hassan N, Tan TC, Spadiut O, Pisanelli I, Fusco L, Haltrich D, Peterbauer CK, Divne C FEBS Open Bio. 2013 Nov 5;3:496-504. PMID:24282677<ref>PMID:24282677</ref>
-	~~[[4mih]] is~~ a ~~8 chain structure~~. ~~Full crystallographic information is available from [http~~:~~//oca~~.~~weizmann.ac.il~~/~~oca-bin/ocashort?id=4MIH OCA].~~	+

-	==~~Reference~~==	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~<ref group="xtra">PMID:024282677</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	</div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Pyranose oxidase]]		[[Category: Pyranose oxidase]]
-	[[Category: Divne, C.]]	+	[[Category: Divne, C]]
-	[[Category: Fusco, L.]]	+	[[Category: Fusco, L]]
-	[[Category: Haltrich, D.]]	+	[[Category: Haltrich, D]]
-	[[Category: Hassan, N.]]	+	[[Category: Hassan, N]]
-	[[Category: Peterbauer, C.]]	+	[[Category: Peterbauer, C]]
-	[[Category: Pisanelli, I.]]	+	[[Category: Pisanelli, I]]
-	[[Category: Spadiut, O.]]	+	[[Category: Spadiut, O]]
-	[[Category: Tan, T C.]]	+	[[Category: Tan, T C]]
	[[Category: Flavinylation]]		[[Category: Flavinylation]]
	[[Category: Gmc oxidoreductase]]		[[Category: Gmc oxidoreductase]]

OCA at 13:34, 11 December 2013

OCA — Wed, 11 Dec 2013 13:34:41 GMT

←Older revision		Revision as of 13:34, 11 December 2013
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-	~~'''Unreleased~~ structure~~'''~~	+	{{Large structure}}
		+	{{STRUCTURE_4mih\| PDB=4mih \| SCENE= }}
		+	===Pyranose 2-oxidase from Phanerochaete chrysosporium, recombinant H158A mutant===
		+	{{ABSTRACT_PUBMED_24282677}}

-	The ~~entry 4mih~~ is ~~ON HOLD~~ ~~until Paper Publication~~	+	==Function==
		+	[[http://www.uniprot.org/uniprot/P2OX_PHACH P2OX_PHACH]] 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. The preferred substrate is D-glucose which is converted to 2-dehydro-D-glucose, an intermediate of a secondary metabolic pathway leading to the antibiotic cortalcerone. Acts also on D-xylose, together with D-glucose the major sugars derived from wood, on L-sorbose, D-galactose and 1,5-anhydroglucitol, a diagnostic marker of diabetes mellitus.<ref>PMID:9210340</ref> <ref>PMID:8661938</ref>

-	~~Authors~~: ~~Hassan, N., Tan, T.C., Spadiut, O., Pisanelli, I., Fusco, L~~.~~, Haltrich, D~~.~~, Peterbauer, C~~.~~, Divne, C~~.	+	==About this Structure==
		+	[[4mih]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MIH OCA].

-	~~Description~~: Pyranose 2-oxidase ~~from Phanerochaete chrysosporium~~, ~~recombinant H158A mutant~~	+	==Reference==
		+	<ref group="xtra">PMID:024282677</ref><references group="xtra"/><references/>
		+	[[Category: Pyranose oxidase]]
		+	[[Category: Divne, C.]]
		+	[[Category: Fusco, L.]]
		+	[[Category: Haltrich, D.]]
		+	[[Category: Hassan, N.]]
		+	[[Category: Peterbauer, C.]]
		+	[[Category: Pisanelli, I.]]
		+	[[Category: Spadiut, O.]]
		+	[[Category: Tan, T C.]]
		+	[[Category: Flavinylation]]
		+	[[Category: Gmc oxidoreductase]]
		+	[[Category: Homotetramer]]
		+	[[Category: Hyphae]]
		+	[[Category: Oxidoreductase]]
		+	[[Category: Phbh fold]]
		+	[[Category: Pyranose 2-oxidaser oxidoreductase]]
		+	[[Category: Rossmann fold]]

OCA at 07:25, 16 October 2013

OCA — Wed, 16 Oct 2013 07:25:07 GMT

←Older revision		Revision as of 07:25, 16 October 2013
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4mih is ON HOLD	+	The entry 4mih is ON HOLD until Paper Publication

	Authors: Hassan, N., Tan, T.C., Spadiut, O., Pisanelli, I., Fusco, L., Haltrich, D., Peterbauer, C., Divne, C.		Authors: Hassan, N., Tan, T.C., Spadiut, O., Pisanelli, I., Fusco, L., Haltrich, D., Peterbauer, C., Divne, C.

	Description: Pyranose 2-oxidase from Phanerochaete chrysosporium, recombinant H158A mutant		Description: Pyranose 2-oxidase from Phanerochaete chrysosporium, recombinant H158A mutant

OCA: Protected "4mih" [edit=sysop:move=sysop]

OCA — Thu, 12 Sep 2013 04:52:03 GMT

Protected "4mih" [edit=sysop:move=sysop]

←Older revision

Revision as of 04:52, 12 September 2013

OCA: New page: '''Unreleased structure''' The entry 4mih is ON HOLD Authors: Hassan, N., Tan, T.C., Spadiut, O., Pisanelli, I., Fusco, L., Haltrich, D., Peterbauer, C., Divne, C. Description: Pyranos...

OCA — Thu, 12 Sep 2013 04:52:02 GMT

New page: '''Unreleased structure''' The entry 4mih is ON HOLD Authors: Hassan, N., Tan, T.C., Spadiut, O., Pisanelli, I., Fusco, L., Haltrich, D., Peterbauer, C., Divne, C. Description: Pyranos...

New page

'''Unreleased structure'''

The entry 4mih is ON HOLD

Authors: Hassan, N., Tan, T.C., Spadiut, O., Pisanelli, I., Fusco, L., Haltrich, D., Peterbauer, C., Divne, C.

Description: Pyranose 2-oxidase from Phanerochaete chrysosporium, recombinant H158A mutant