3lsh - Revision history

OCA at 10:22, 21 February 2024

2024-02-21T10:22:16Z

←Older revision		Revision as of 10:22, 21 February 2024
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	<StructureSection load='3lsh' size='340' side='right'caption='[[3lsh]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='3lsh' size='340' side='right'caption='[[3lsh]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3lsh]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Coriolus_zonatus Coriolus zonatus~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LSH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LSH FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3lsh]] 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=3LSH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LSH 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=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</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]] 1.9Å</td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>~~[[~~Related_structure~~\|~~Related:~~]]~~</b></td><td class="sblockDat"><div style='overflow: auto~~; ~~max-height: 3em;'>[[3lsi\|3lsi]], [[3lsk\|3lsk]], [[3lsm\|3lsm]]</div>~~</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=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene></td></tr>
-	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat"~~>p2o ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&~~id=~~230624 Coriolus zonatus])</td~~><~~/tr>~~	+
-	~~<tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b~~></td><~~td class~~=~~"sblockDat"><span class~~=~~'plainlinks~~'>~~[https://en.wikipedia.org/wiki/Pyranose_oxidase Pyranose oxidase], with EC number [https://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'>[https://proteopedia.org/fgij/fg.htm?mol=3lsh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lsh OCA], [https://pdbe.org/3lsh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3lsh RCSB], [https://www.ebi.ac.uk/pdbsum/3lsh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3lsh 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=3lsh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lsh OCA], [https://pdbe.org/3lsh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3lsh RCSB], [https://www.ebi.ac.uk/pdbsum/3lsh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3lsh ProSAT]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/Q7ZA32_TRAOC Q7ZA32_TRAOC]
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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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=3lsh ConSurf].		</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=3lsh ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Flavoenzymes perform a wide range of redox reactions in nature, and a subclass of flavoenzymes carry covalently bound cofactor. The enzyme-flavin bond helps to increase the flavin's redox potential to facilitate substrate oxidation in several oxidases. The formation of the enzyme-flavin covalent bond--the flavinylation reaction--has been studied for the past 40 years. For the most advocated mechanism of autocatalytic flavinylation, the quinone methide mechanism, appropriate stabilization of developing negative charges at the flavin N(1) and N(5) loci is crucial. Whereas the structural basis for stabilization at N(1) is relatively well studied, the structural requisites for charge stabilization at N(5) remain less clear. Here, we show that flavinylation of histidine 167 of pyranose 2-oxidase from Trametes multicolor requires hydrogen bonding at the flavin N(5)/O(4) locus, which is offered by the side chain of Thr169 when the enzyme is in its closed, but not open, state. Moreover, our data show that additional stabilization at N(5) by histidine 548 is required to ensure high occupancy of the histidyl-flavin bond. The combination of structural and spectral data on pyranose 2-oxidase mutants supports the quinone methide mechanism. Our results demonstrate an elaborate structural fine-tuning of the active site to complete its own formation that couples efficient holoenzyme synthesis to conformational substates of the substrate-recognition loop and concerted movements of side chains near the flavinylation ligand.
-
-	H-bonding and positive charge at the N5/O4 locus are critical for covalent flavin attachment in trametes pyranose 2-oxidase.,Tan TC, Pitsawong W, Wongnate T, Spadiut O, Haltrich D, Chaiyen P, Divne C J Mol Biol. 2010 Sep 24;402(3):578-94. Epub 2010 Aug 12. PMID:20708626<ref>PMID:20708626</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 3lsh" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Pyranose oxidase\|Pyranose oxidase]]		*[[Pyranose oxidase\|Pyranose oxidase]]
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Coriolus zonatus]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Pyranose oxidase~~]]	+	[[Category: Trametes ochracea]]
-	[[Category: Divne, C]]	+	[[Category: Divne C]]
-	[[Category: Spadiut, O]]	+	[[Category: Spadiut O]]
-	[[Category: Tan~~, T C]]~~	+	[[Category: Tan TC]]
-	~~[[Category: Gmc oxidoreductase]]~~	+
-	~~[[Category: Homotetramer]]~~	+
-	~~[[Category: Non-covalent fad]]~~	+
-	~~[[Category: Oxidoreductase]]~~	+
-	~~[[Category: Phbh fold]]~~	+
-	~~[[Category: Rossmann fold]]~~	+
-	~~[[Category: T169a mutant~~]]	+

OCA at 12:38, 13 October 2021

2021-10-13T12:38:26Z

←Older revision		Revision as of 12:38, 13 October 2021
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	==Pyranose 2-oxidase T169A, monoclinic==		==Pyranose 2-oxidase T169A, monoclinic==
-	<StructureSection load='3lsh' size='340' side='right' caption='[[3lsh]], [[Resolution\|resolution]] 1.90Å' scene=''>	+	<StructureSection load='3lsh' size='340' side='right'caption='[[3lsh]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3lsh]] is a 4 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Coriolus_zonatus Coriolus zonatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LSH OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3LSH FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3lsh]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Coriolus_zonatus Coriolus zonatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LSH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LSH 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=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</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=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3lsi\|3lsi]], [[3lsk\|3lsk]], [[3lsm\|3lsm]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3lsi\|3lsi]], [[3lsk\|3lsk]], [[3lsm\|3lsm]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">p2o ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=230624 Coriolus zonatus])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">p2o ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=230624 Coriolus zonatus])</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'>[https://en.wikipedia.org/wiki/Pyranose_oxidase Pyranose oxidase], with EC number [https://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=3lsh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lsh OCA], [~~http~~://pdbe.org/3lsh PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3lsh RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3lsh PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3lsh 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=3lsh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lsh OCA], [https://pdbe.org/3lsh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3lsh RCSB], [https://www.ebi.ac.uk/pdbsum/3lsh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3lsh ProSAT]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
Line 14:		Line 14:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ls/3lsh_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ls/3lsh_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
Line 29:		Line 29:
	</div>		</div>
	<div class="pdbe-citations 3lsh" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 3lsh" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Pyranose oxidase\|Pyranose oxidase]]
	== References ==		== References ==
	<references/>		<references/>
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	</StructureSection>		</StructureSection>
	[[Category: Coriolus zonatus]]		[[Category: Coriolus zonatus]]
		+	[[Category: Large Structures]]
	[[Category: Pyranose oxidase]]		[[Category: Pyranose oxidase]]
	[[Category: Divne, C]]		[[Category: Divne, C]]

OCA at 09:02, 1 November 2017

2017-11-01T09:02:24Z

←Older revision		Revision as of 09:02, 1 November 2017
Line 29:		Line 29:
	</div>		</div>
	<div class="pdbe-citations 3lsh" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 3lsh" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Pyranose oxidase\|Pyranose oxidase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 19:49, 5 August 2016

2016-08-05T19:49:14Z

←Older revision		Revision as of 19:49, 5 August 2016
Line 1:		Line 1:
		+
	==Pyranose 2-oxidase T169A, monoclinic==		==Pyranose 2-oxidase T169A, monoclinic==
	<StructureSection load='3lsh' size='340' side='right' caption='[[3lsh]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='3lsh' size='340' side='right' caption='[[3lsh]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3lsh]] is a 4 chain structure with 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=3LSH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LSH FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3lsh]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Coriolus_zonatus Coriolus zonatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LSH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LSH 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=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene></td></tr>		</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=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3lsi\|3lsi]], [[3lsk\|3lsk]], [[3lsm\|3lsm]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3lsi\|3lsi]], [[3lsk\|3lsk]], [[3lsm\|3lsm]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">p2o ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=230624 ~~Trametes ochracea~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">p2o ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=230624 Coriolus zonatus])</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=3lsh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lsh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3lsh RCSB], [http://www.ebi.ac.uk/pdbsum/3lsh 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=3lsh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lsh OCA], [http://pdbe.org/3lsh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3lsh RCSB], [http://www.ebi.ac.uk/pdbsum/3lsh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3lsh ProSAT]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
Line 17:		Line 18:
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</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/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].	+	</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=3lsh ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 27:		Line 28:
	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 3lsh" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Pyranose oxidase\|Pyranose oxidase]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Coriolus zonatus]]
	[[Category: Pyranose oxidase]]		[[Category: Pyranose oxidase]]
-	[[Category: Trametes ochracea]]
	[[Category: Divne, C]]		[[Category: Divne, C]]
	[[Category: Spadiut, O]]		[[Category: Spadiut, O]]

OCA at 15:54, 18 December 2014

2014-12-18T15:54:52Z

←Older revision		Revision as of 15:54, 18 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_3lsh\| PDB~~=3lsh \| ~~SCENE~~= }}	+	==Pyranose 2-oxidase T169A, monoclinic==
-	===~~Pyranose~~ 2-oxidase ~~T169A~~, ~~monoclinic~~===	+	<StructureSection load='3lsh' size='340' side='right' caption='[[3lsh]], [[Resolution\|resolution]] 1.90Å' scene=''>
-	~~{{ABSTRACT_PUBMED_20708626}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3lsh]] is a 4 chain structure with 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=3LSH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LSH 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=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3lsi\|3lsi]], [[3lsk\|3lsk]], [[3lsm\|3lsm]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">p2o ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=230624 Trametes ochracea])</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=3lsh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lsh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3lsh RCSB], [http://www.ebi.ac.uk/pdbsum/3lsh PDBsum]</span></td></tr>
		+	</table>
		+	== 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/ls/3lsh_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/chain_selection.php?pdb_ID=2ata ConSurf].
		+	<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Flavoenzymes perform a wide range of redox reactions in nature, and a subclass of flavoenzymes carry covalently bound cofactor. The enzyme-flavin bond helps to increase the flavin's redox potential to facilitate substrate oxidation in several oxidases. The formation of the enzyme-flavin covalent bond--the flavinylation reaction--has been studied for the past 40 years. For the most advocated mechanism of autocatalytic flavinylation, the quinone methide mechanism, appropriate stabilization of developing negative charges at the flavin N(1) and N(5) loci is crucial. Whereas the structural basis for stabilization at N(1) is relatively well studied, the structural requisites for charge stabilization at N(5) remain less clear. Here, we show that flavinylation of histidine 167 of pyranose 2-oxidase from Trametes multicolor requires hydrogen bonding at the flavin N(5)/O(4) locus, which is offered by the side chain of Thr169 when the enzyme is in its closed, but not open, state. Moreover, our data show that additional stabilization at N(5) by histidine 548 is required to ensure high occupancy of the histidyl-flavin bond. The combination of structural and spectral data on pyranose 2-oxidase mutants supports the quinone methide mechanism. Our results demonstrate an elaborate structural fine-tuning of the active site to complete its own formation that couples efficient holoenzyme synthesis to conformational substates of the substrate-recognition loop and concerted movements of side chains near the flavinylation ligand.

-	~~==About this Structure==~~	+	H-bonding and positive charge at the N5/O4 locus are critical for covalent flavin attachment in trametes pyranose 2-oxidase.,Tan TC, Pitsawong W, Wongnate T, Spadiut O, Haltrich D, Chaiyen P, Divne C J Mol Biol. 2010 Sep 24;402(3):578-94. Epub 2010 Aug 12. PMID:20708626<ref>PMID:20708626</ref>
-	~~[[3lsh]] is a 4 chain structure with 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=3LSH OCA].~~	+

-	==~~Reference~~==	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~<ref group="xtra">PMID:020708626</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	</div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Pyranose oxidase]]		[[Category: Pyranose oxidase]]
	[[Category: Trametes ochracea]]		[[Category: Trametes ochracea]]
-	[[Category: Divne, C.]]	+	[[Category: Divne, C]]
-	[[Category: Spadiut, O.]]	+	[[Category: Spadiut, O]]
-	[[Category: Tan, T C.]]	+	[[Category: Tan, T C]]
	[[Category: Gmc oxidoreductase]]		[[Category: Gmc oxidoreductase]]
	[[Category: Homotetramer]]		[[Category: Homotetramer]]

OCA: Protected "3lsh" [edit=sysop:move=sysop]

2013-04-10T23:15:23Z

Protected "3lsh" [edit=sysop:move=sysop]

←Older revision

Revision as of 23:15, 10 April 2013

OCA at 23:15, 10 April 2013

2013-04-10T23:15:21Z

←Older revision		Revision as of 23:15, 10 April 2013
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-	{{Seed}}
-	[[Image:3lsh.png\|left\|200px]]
-
-	<!--
-	The line below this paragraph, containing "STRUCTURE_3lsh", creates the "Structure Box" on the page.
-	You may change the PDB parameter (which sets the PDB file loaded into the applet)
-	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-	or leave the SCENE parameter empty for the default display.
-	-->
	{{STRUCTURE_3lsh\| PDB=3lsh \| SCENE= }}		{{STRUCTURE_3lsh\| PDB=3lsh \| SCENE= }}
-
	===Pyranose 2-oxidase T169A, monoclinic===		===Pyranose 2-oxidase T169A, monoclinic===
-
-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_20708626}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 20708626 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_20708626}}		{{ABSTRACT_PUBMED_20708626}}

	==About this Structure==		==About this Structure==
-	~~3LSH~~ is a 4 ~~chains~~ structure with ~~sequences~~ 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=3LSH OCA].	+	[[3lsh]] is a 4 chain structure with 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=3LSH OCA].

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~20708626~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:020708626</ref><references group="xtra"/><references/>
	[[Category: Pyranose oxidase]]		[[Category: Pyranose oxidase]]
	[[Category: Trametes ochracea]]		[[Category: Trametes ochracea]]
Line 36:		Line 20:
	[[Category: Rossmann fold]]		[[Category: Rossmann fold]]
	[[Category: T169a mutant]]		[[Category: T169a mutant]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Nov 24 13:40:58 2010''

OCA at 10:29, 24 November 2010

2010-11-24T10:29:28Z

←Older revision		Revision as of 10:29, 24 November 2010
Line 1:		Line 1:
	{{Seed}}		{{Seed}}
-	[[Image:3lsh.~~jpg~~\|left\|200px]]	+	[[Image:3lsh.png\|left\|200px]]

	<!--		<!--
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	===Pyranose 2-oxidase T169A, monoclinic===		===Pyranose 2-oxidase T169A, monoclinic===

		+
		+	<!--
		+	The line below this paragraph, {{ABSTRACT_PUBMED_20708626}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 20708626 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_20708626}}

	==About this Structure==		==About this Structure==
	3LSH is a 4 chains structure with sequences 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=3LSH OCA].		3LSH is a 4 chains structure with sequences 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=3LSH OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:20708626</ref><references group="xtra"/>
	[[Category: Pyranose oxidase]]		[[Category: Pyranose oxidase]]
	[[Category: Trametes ochracea]]		[[Category: Trametes ochracea]]
Line 28:		Line 37:
	[[Category: T169a mutant]]		[[Category: T169a mutant]]

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed ~~Aug 25 08~~:57:32 2010''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Nov 24 13:40:58 2010''

OCA at 04:49, 25 August 2010

2010-08-25T04:49:43Z

←Older revision		Revision as of 04:49, 25 August 2010
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	{{Seed}}
		+	[[Image:3lsh.jpg\|left\|200px]]

-	The ~~entry 3lsh~~ is ~~ON HOLD~~ ~~until Paper Publication~~	+	<!--
		+	The line below this paragraph, containing "STRUCTURE_3lsh", creates the "Structure Box" on the page.
		+	You may change the PDB parameter (which sets the PDB file loaded into the applet)
		+	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
		+	or leave the SCENE parameter empty for the default display.
		+	-->
		+	{{STRUCTURE_3lsh\| PDB=3lsh \| SCENE= }}

-	~~Authors: Divne~~, ~~C., Tan, T.C., Spadiut, O.~~	+	===Pyranose 2-oxidase T169A, monoclinic===

-	Description: Pyranose 2-oxidase T169A, monoclinic

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed ~~Mar 10 13~~:14:47 2010''	+	==About this Structure==
		+	3LSH is a 4 chains structure with sequences 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=3LSH OCA].
		+	[[Category: Pyranose oxidase]]
		+	[[Category: Trametes ochracea]]
		+	[[Category: Divne, C.]]
		+	[[Category: Spadiut, O.]]
		+	[[Category: Tan, T C.]]
		+	[[Category: Gmc oxidoreductase]]
		+	[[Category: Homotetramer]]
		+	[[Category: Non-covalent fad]]
		+	[[Category: Oxidoreductase]]
		+	[[Category: Phbh fold]]
		+	[[Category: Rossmann fold]]
		+	[[Category: T169a mutant]]
		+
		+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Aug 25 08:57:32 2010''

OCA at 11:14, 10 March 2010

2010-03-10T11:14:48Z

←Older revision		Revision as of 11:14, 10 March 2010
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 3lsh is ON HOLD	+	The entry 3lsh is ON HOLD until Paper Publication

	Authors: Divne, C., Tan, T.C., Spadiut, O.		Authors: Divne, C., Tan, T.C., Spadiut, O.
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	Description: Pyranose 2-oxidase T169A, monoclinic		Description: Pyranose 2-oxidase T169A, monoclinic

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Thu Feb 25~~ 13:04:39 2010''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar 10 13:14:47 2010''