4fef - Revision history

OCA at 02:52, 21 November 2024

2024-11-21T02:52:50Z

← Older revision		Revision as of 02:52, 21 November 2024
Line 10:		Line 10:
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/VPL2_PLEER VPL2_PLEER] A versatile ligninolytic peroxidase that combines the substrate specificity characteristics of the two other ligninolytic peroxidases, manganese peroxidase and lignin peroxidase.<ref>PMID:9987124</ref>		[https://www.uniprot.org/uniprot/VPL2_PLEER VPL2_PLEER] A versatile ligninolytic peroxidase that combines the substrate specificity characteristics of the two other ligninolytic peroxidases, manganese peroxidase and lignin peroxidase.<ref>PMID:9987124</ref>
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			Versatile peroxidase shares with manganese peroxidase and lignin peroxidase the ability to oxidize Mn(2+) and high redox potential aromatic compounds, respectively. Moreover, it is also able to oxidize phenols (and low redox potential dyes) at two catalytic sites, as shown by biphasic kinetics. A high efficiency site (with 2,6-dimethoxyphenol and p-hydroquinone catalytic efficiencies of approximately 70 and approximately 700 s(-1) mm(-1), respectively) was localized at the same exposed Trp-164 responsible for high redox potential substrate oxidation (as shown by activity loss in the W164S variant). The second site, characterized by low catalytic efficiency ( approximately 3 and approximately 50 s(-1) mm(-1) for 2,6-dimethoxyphenol and p-hydroquinone, respectively) was localized at the main heme access channel. Steady-state and transient-state kinetics for oxidation of phenols and dyes at the latter site were improved when side chains of residues forming the heme channel edge were removed in single and multiple variants. Among them, the E140G/K176G, E140G/P141G/K176G, and E140G/W164S/K176G variants attained catalytic efficiencies for oxidation of 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonate) at the heme channel similar to those of the exposed tryptophan site. The heme channel enlargement shown by x-ray diffraction of the E140G, P141G, K176G, and E140G/K176G variants would allow a better substrate accommodation near the heme, as revealed by the up to 26-fold lower K(m) values (compared with native VP). The resulting interactions were shown by the x-ray structure of the E140G-guaiacol complex, which includes two H-bonds of the substrate with Arg-43 and Pro-139 in the distal heme pocket (at the end of the heme channel) and several hydrophobic interactions with other residues and the heme cofactor.

			Two Oxidation Sites for Low Redox Potential Substrates: A DIRECTED MUTAGENESIS, KINETIC, AND CRYSTALLOGRAPHIC STUDY ON PLEUROTUS ERYNGII VERSATILE PEROXIDASE.,Morales M, Mate MJ, Romero A, Martinez MJ, Martinez AT, Ruiz-Duenas FJ J Biol Chem. 2012 Nov 30;287(49):41053-67. doi: 10.1074/jbc.M112.405548. Epub, 2012 Oct 15. PMID:23071108<ref>PMID:23071108</ref>

			From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>
			<div class="pdbe-citations 4fef" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 15:23, 14 March 2024

2024-03-14T15:23:06Z

← Older revision		Revision as of 15:23, 14 March 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4fef]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pleurotus_eryngii Pleurotus eryngii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FEF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FEF FirstGlance]. <br>		<table><tr><td colspan='2'>[[4fef]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pleurotus_eryngii Pleurotus eryngii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FEF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FEF FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2Å</td></tr>
			<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4fef FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fef OCA], [https://pdbe.org/4fef PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fef RCSB], [https://www.ebi.ac.uk/pdbsum/4fef PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fef 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=4fef FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fef OCA], [https://pdbe.org/4fef PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fef RCSB], [https://www.ebi.ac.uk/pdbsum/4fef PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fef ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/VPL2_PLEER VPL2_PLEER] A versatile ligninolytic peroxidase that combines the substrate specificity characteristics of the two other ligninolytic peroxidases, manganese peroxidase and lignin peroxidase.<ref>PMID:9987124</ref>		[https://www.uniprot.org/uniprot/VPL2_PLEER VPL2_PLEER] A versatile ligninolytic peroxidase that combines the substrate specificity characteristics of the two other ligninolytic peroxidases, manganese peroxidase and lignin peroxidase.<ref>PMID:9987124</ref>
	~~<div style="background-color:#fffaf0;">~~
	~~== Publication Abstract from PubMed ==~~
	Versatile peroxidase shares with manganese peroxidase and lignin peroxidase the ability to oxidize Mn(2+) and high redox potential aromatic compounds, respectively. Moreover, it is also able to oxidize phenols (and low redox potential dyes) at two catalytic sites, as shown by biphasic kinetics. A high efficiency site (with 2,6-dimethoxyphenol and p-hydroquinone catalytic efficiencies of approximately 70 and approximately 700 s(-1) mm(-1), respectively) was localized at the same exposed Trp-164 responsible for high redox potential substrate oxidation (as shown by activity loss in the W164S variant). The second site, characterized by low catalytic efficiency ( approximately 3 and approximately 50 s(-1) mm(-1) for 2,6-dimethoxyphenol and p-hydroquinone, respectively) was localized at the main heme access channel. Steady-state and transient-state kinetics for oxidation of phenols and dyes at the latter site were improved when side chains of residues forming the heme channel edge were removed in single and multiple variants. Among them, the E140G/K176G, E140G/P141G/K176G, and E140G/W164S/K176G variants attained catalytic efficiencies for oxidation of 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonate) at the heme channel similar to those of the exposed tryptophan site. The heme channel enlargement shown by x-ray diffraction of the E140G, P141G, K176G, and E140G/K176G variants would allow a better substrate accommodation near the heme, as revealed by the up to 26-fold lower K(m) values (compared with native VP). The resulting interactions were shown by the x-ray structure of the E140G-guaiacol complex, which includes two H-bonds of the substrate with Arg-43 and Pro-139 in the distal heme pocket (at the end of the heme channel) and several hydrophobic interactions with other residues and the heme cofactor.

	Two Oxidation Sites for Low Redox Potential Substrates: A DIRECTED MUTAGENESIS, KINETIC, AND CRYSTALLOGRAPHIC STUDY ON PLEUROTUS ERYNGII VERSATILE PEROXIDASE.,Morales M, Mate MJ, Romero A, Martinez MJ, Martinez AT, Ruiz-Duenas FJ J Biol Chem. 2012 Nov 30;287(49):41053-67. doi: 10.1074/jbc.M112.405548. Epub, 2012 Oct 15. PMID:23071108<ref>PMID:23071108</ref>

	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~
	~~</div>~~
	~~<div class="pdbe-citations 4fef" style="background-color:#fffaf0;"></div>~~
	== References ==		== References ==
	<references/>		<references/>

OCA at 04:51, 7 October 2022

2022-10-07T04:51:44Z

← Older revision		Revision as of 04:51, 7 October 2022
Line 1:		Line 1:

	==The crystal structures of several mutants of pleurotus eryngii versatile peroxidase==		==The crystal structures of several mutants of pleurotus eryngii versatile peroxidase==
	<StructureSection load='4fef' size='340' side='right' caption='[[4fef]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='4fef' size='340' side='right'caption='[[4fef]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4fef]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Boletus_of_the_steppes Boletus of the steppes~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FEF OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4FEF FirstGlance]. <br>		<table><tr><td colspan='2'>[[4fef]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pleurotus_eryngii Pleurotus eryngii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FEF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FEF FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene~~></td></tr>~~		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4fcs\|4fcs]], [[4fcn\|4fcn]], [[4fdq\|4fdq]]</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=4fef FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fef OCA], [https://pdbe.org/4fef PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fef RCSB], [https://www.ebi.ac.uk/pdbsum/4fef PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fef ProSAT]</span></td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">vpl2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5323 Boletus of the steppes])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Versatile_peroxidase Versatile peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.16 1.11.1.16] </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=4fef FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fef OCA], [~~http~~://pdbe.org/4fef PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4fef RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4fef PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4fef ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[~~[http~~://www.uniprot.org/uniprot/VPL2_PLEER VPL2_PLEER]] A versatile ligninolytic peroxidase that combines the substrate specificity characteristics of the two other ligninolytic peroxidases, manganese peroxidase and lignin peroxidase.<ref>PMID:9987124</ref>		[https://www.uniprot.org/uniprot/VPL2_PLEER VPL2_PLEER] A versatile ligninolytic peroxidase that combines the substrate specificity characteristics of the two other ligninolytic peroxidases, manganese peroxidase and lignin peroxidase.<ref>PMID:9987124</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 25:		Line 22:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Boletus of the steppes~~]]		[[Category: Large Structures]]
	[[Category: ~~Versatile peroxidase~~]]		[[Category: Pleurotus eryngii]]
	[[Category: Martinez~~, A T~~]]		[[Category: Martinez AT]]
	[[Category: Mate~~, M J~~]]		[[Category: Mate MJ]]
	[[Category: Romero, A]]		[[Category: Romero A]]
	[[Category: Ruiz-Duenas~~, F J]]~~		[[Category: Ruiz-Duenas FJ]]
	~~[[Category: Aromatic-substrate binding]]~~
	~~[[Category: Lignin degradation]]~~
	~~[[Category: Lignin peroxidase]]~~
	~~[[Category: Oxidoreductase~~]]

OCA at 21:19, 5 August 2016

2016-08-05T21:19:25Z

← Older revision		Revision as of 21:19, 5 August 2016
Line 1:		Line 1:

	==The crystal structures of several mutants of pleurotus eryngii versatile peroxidase==		==The crystal structures of several mutants of pleurotus eryngii versatile peroxidase==
	<StructureSection load='4fef' size='340' side='right' caption='[[4fef]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='4fef' size='340' side='right' caption='[[4fef]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4fef]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Pleurotus_eryngii Pleurotus eryngii~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FEF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FEF FirstGlance]. <br>		<table><tr><td colspan='2'>[[4fef]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Boletus_of_the_steppes Boletus of the steppes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FEF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FEF FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4fcs\|4fcs]], [[4fcn\|4fcn]], [[4fdq\|4fdq]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4fcs\|4fcs]], [[4fcn\|4fcn]], [[4fdq\|4fdq]]</td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">vpl2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5323 ~~Pleurotus eryngii~~])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">vpl2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5323 Boletus of the steppes])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Versatile_peroxidase Versatile peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.16 1.11.1.16] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Versatile_peroxidase Versatile peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.16 1.11.1.16] </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=4fef FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fef OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4fef RCSB], [http://www.ebi.ac.uk/pdbsum/4fef 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=4fef FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fef OCA], [http://pdbe.org/4fef PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4fef RCSB], [http://www.ebi.ac.uk/pdbsum/4fef PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4fef ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 19:		Line 20:
	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 4fef" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Pleurotus eryngii~~]]		[[Category: Boletus of the steppes]]
	[[Category: Versatile peroxidase]]		[[Category: Versatile peroxidase]]
	[[Category: Martinez, A T]]		[[Category: Martinez, A T]]

OCA at 05:59, 25 December 2014

2014-12-25T05:59:08Z

← Older revision		Revision as of 05:59, 25 December 2014
Line 9:		Line 9:
	<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=4fef FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fef OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4fef RCSB], [http://www.ebi.ac.uk/pdbsum/4fef 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=4fef FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fef OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4fef RCSB], [http://www.ebi.ac.uk/pdbsum/4fef PDBsum]</span></td></tr>
	</table>		</table>
			== Function ==
			[[http://www.uniprot.org/uniprot/VPL2_PLEER VPL2_PLEER]] A versatile ligninolytic peroxidase that combines the substrate specificity characteristics of the two other ligninolytic peroxidases, manganese peroxidase and lignin peroxidase.<ref>PMID:9987124</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 14:58, 9 December 2014

2014-12-09T14:58:38Z

← Older revision		Revision as of 14:58, 9 December 2014
Line 1:		Line 1:
	[[~~Image~~:~~4fef~~.~~png~~\|~~left~~\|~~200px~~]]		==The crystal structures of several mutants of pleurotus eryngii versatile peroxidase==
			<StructureSection load='4fef' size='340' side='right' caption='[[4fef]], [[Resolution\|resolution]] 2.00Å' scene=''>
			== Structural highlights ==
			<table><tr><td colspan='2'>[[4fef]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pleurotus_eryngii Pleurotus eryngii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FEF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FEF FirstGlance]. <br>
			</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
			<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4fcs\|4fcs]], [[4fcn\|4fcn]], [[4fdq\|4fdq]]</td></tr>
			<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">vpl2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5323 Pleurotus eryngii])</td></tr>
			<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Versatile_peroxidase Versatile peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.16 1.11.1.16] </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=4fef FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fef OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4fef RCSB], [http://www.ebi.ac.uk/pdbsum/4fef PDBsum]</span></td></tr>
			</table>
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			Versatile peroxidase shares with manganese peroxidase and lignin peroxidase the ability to oxidize Mn(2+) and high redox potential aromatic compounds, respectively. Moreover, it is also able to oxidize phenols (and low redox potential dyes) at two catalytic sites, as shown by biphasic kinetics. A high efficiency site (with 2,6-dimethoxyphenol and p-hydroquinone catalytic efficiencies of approximately 70 and approximately 700 s(-1) mm(-1), respectively) was localized at the same exposed Trp-164 responsible for high redox potential substrate oxidation (as shown by activity loss in the W164S variant). The second site, characterized by low catalytic efficiency ( approximately 3 and approximately 50 s(-1) mm(-1) for 2,6-dimethoxyphenol and p-hydroquinone, respectively) was localized at the main heme access channel. Steady-state and transient-state kinetics for oxidation of phenols and dyes at the latter site were improved when side chains of residues forming the heme channel edge were removed in single and multiple variants. Among them, the E140G/K176G, E140G/P141G/K176G, and E140G/W164S/K176G variants attained catalytic efficiencies for oxidation of 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonate) at the heme channel similar to those of the exposed tryptophan site. The heme channel enlargement shown by x-ray diffraction of the E140G, P141G, K176G, and E140G/K176G variants would allow a better substrate accommodation near the heme, as revealed by the up to 26-fold lower K(m) values (compared with native VP). The resulting interactions were shown by the x-ray structure of the E140G-guaiacol complex, which includes two H-bonds of the substrate with Arg-43 and Pro-139 in the distal heme pocket (at the end of the heme channel) and several hydrophobic interactions with other residues and the heme cofactor.

	~~{{STRUCTURE_4fef\| PDB=4fef \| SCENE= }}~~		Two Oxidation Sites for Low Redox Potential Substrates: A DIRECTED MUTAGENESIS, KINETIC, AND CRYSTALLOGRAPHIC STUDY ON PLEUROTUS ERYNGII VERSATILE PEROXIDASE.,Morales M, Mate MJ, Romero A, Martinez MJ, Martinez AT, Ruiz-Duenas FJ J Biol Chem. 2012 Nov 30;287(49):41053-67. doi: 10.1074/jbc.M112.405548. Epub, 2012 Oct 15. PMID:23071108<ref>PMID:23071108</ref>

	~~===The crystal structures of several mutants~~ of ~~pleurotus eryngii versatile peroxidase===~~		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>
	~~{{ABSTRACT_PUBMED_23071108}}~~		== References ==
			<references/>
	~~==About this Structure==~~		__TOC__
	~~[[4fef]] is a 1 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Pleurotus_eryngii Pleurotus eryngii]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=4FEF OCA].~~		</StructureSection>

	==~~Reference~~==
	<~~ref group="xtra">PMID:018201105<~~/~~ref~~><~~references group="xtra"~~/>
	[[Category: Pleurotus eryngii]]		[[Category: Pleurotus eryngii]]
	[[Category: Versatile peroxidase]]		[[Category: Versatile peroxidase]]
	[[Category: Martinez, A T.]]		[[Category: Martinez, A T]]
	[[Category: Mate, M J.]]		[[Category: Mate, M J]]
	[[Category: Romero, A.]]		[[Category: Romero, A]]
	[[Category: Ruiz-Duenas, F J.]]		[[Category: Ruiz-Duenas, F J]]
	[[Category: Aromatic-substrate binding]]		[[Category: Aromatic-substrate binding]]
	[[Category: Lignin degradation]]		[[Category: Lignin degradation]]
	[[Category: Lignin peroxidase]]		[[Category: Lignin peroxidase]]
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]

OCA at 10:28, 19 December 2012

2012-12-19T10:28:32Z

← Older revision		Revision as of 10:28, 19 December 2012
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	[[Image:4fef.~~jpg~~\|left\|200px]]		[[Image:4fef.png\|left\|200px]]

	{{STRUCTURE_4fef\| PDB=4fef \| SCENE= }}		{{STRUCTURE_4fef\| PDB=4fef \| SCENE= }}
Line 5:		Line 5:
	===The crystal structures of several mutants of pleurotus eryngii versatile peroxidase===		===The crystal structures of several mutants of pleurotus eryngii versatile peroxidase===

	{{~~ABSTRACT_PUBMED_18201105~~}}		{{ABSTRACT_PUBMED_23071108}}

	==About this Structure==		==About this Structure==

OCA at 07:44, 24 October 2012

2012-10-24T07:44:42Z

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
+[[Image:4fef.jpg|left|200px]]
-The entry 4fef is ON HOLD  until Paper Publication
+{{STRUCTURE_4fef|  PDB=4fef  |  SCENE=  }}
-Authors: Mate, M.J., Romero, A., Ruiz-Duenas, F.J., Martinez, A.T.
+===The crystal structures of several mutants of pleurotus eryngii versatile peroxidase===
-Description: The crystal structures of several mutants of pleurotus eryngii versatile peroxidase
+{{ABSTRACT_PUBMED_18201105}}

OCA at 05:23, 27 June 2012

2012-06-27T05:23:38Z

← Older revision		Revision as of 05:23, 27 June 2012
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

	The entry 4fef is ON HOLD		The entry 4fef is ON HOLD until Paper Publication

	Authors: Mate, M.J., Romero, A., Ruiz-Duenas, F.J., Martinez, A.T.		Authors: Mate, M.J., Romero, A., Ruiz-Duenas, F.J., Martinez, A.T.

	Description: The crystal structures of several mutants of pleurotus eryngii versatile peroxidase		Description: The crystal structures of several mutants of pleurotus eryngii versatile peroxidase

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

2012-06-06T07:23:05Z

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

← Older revision	Revision as of 07:23, 6 June 2012
(No difference)