3vsh - Revision history

OCA at 12:35, 8 November 2023

OCA — Wed, 08 Nov 2023 12:35:06 GMT

←Older revision		Revision as of 12:35, 8 November 2023
Line 3:		Line 3:
	<StructureSection load='3vsh' size='340' side='right'caption='[[3vsh]], [[Resolution\|resolution]] 2.70Å' scene=''>		<StructureSection load='3vsh' size='340' side='right'caption='[[3vsh]], [[Resolution\|resolution]] 2.70Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3vsh]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Comamonas_testosteroni~~ Comamonas testosteroni]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VSH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VSH FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3vsh]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Comamonas_testosteroni_CNB-1 Comamonas testosteroni CNB-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VSH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VSH FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=FE2:FE+(II)+ION'>FE2</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]] 2.7Å</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"~~><div style='overflow: auto; max-height: 3em;'>[[3vhg\|3vhg]], [[3vhi\|3vhi]], [[3vhj\|3vhj]]</div></td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene></td></tr>
-	~~<tr~~ id~~='activity'><td class~~="~~sblockLbl~~"><~~b>Activity:</b></td><td class~~=~~"sblockDat"><span class~~=~~'plainlinks~~'>~~[https://en.wikipedia.org/wiki/Protocatechuate_4,5-dioxygenase Protocatechuate 4,5-dioxygenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.8 1.13.11.8]~~ </~~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=3vsh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vsh OCA], [https://pdbe.org/3vsh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vsh RCSB], [https://www.ebi.ac.uk/pdbsum/3vsh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vsh 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=3vsh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vsh OCA], [https://pdbe.org/3vsh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vsh RCSB], [https://www.ebi.ac.uk/pdbsum/3vsh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vsh ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/AMNA_COMTE AMNA_COMTE]] Component of the 2-aminophenol 1,6-dioxygenase (APD) complex that catalyzes the ring fission of 2-aminophenol to produce 2-aminomuconic semialdehyde. CnbCa may have a role in the stability of the complex. The complex is also active on other substrates such as 2-amino-5-chlorophenol (68% activity), protocatechuate (33% activity) and catechol (5% activity). Both 2-aminophenol and 2-amino-5-cholorophenol are likely native substrates for this dioxygenase which is involved in the reductive degradation pathway of both nitrobenzene (NB) and 4-chloronitrobenzene (4-CNB), allowing C.testosteroni strain CNB-1 to grow on these compounds as sole source of carbon, nitrogen, and energy.<ref>PMID:15580337</ref> <ref>PMID:16517619</ref> [[https://www.uniprot.org/uniprot/AMNB_COMTE AMNB_COMTE]] Component of the 2-aminophenol 1,6-dioxygenase (APD) complex that catalyzes the ring fission of 2-aminophenol to produce 2-aminomuconic semialdehyde. CnbCb seems to be the catalytic subunit of the complex. Also active on other substrates such as 2-amino-5-chlorophenol (68% activity), protocatechuate (33% activity) and catechol (5% activity). Both 2-aminophenol and 2-amino-5-cholorophenol are likely native substrates for this dioxygenase which is involved in the reductive degradation pathway of both nitrobenzene (NB) and 4-chloronitrobenzene (4-CNB), allowing C.testosteroni strain CNB-1 to grow on these compounds as sole source of carbon, nitrogen, and energy.<ref>PMID:15580337</ref> <ref>PMID:16517619</ref>	+	[https://www.uniprot.org/uniprot/AMNA_COMTE AMNA_COMTE] Component of the 2-aminophenol 1,6-dioxygenase (APD) complex that catalyzes the ring fission of 2-aminophenol to produce 2-aminomuconic semialdehyde. CnbCa may have a role in the stability of the complex. The complex is also active on other substrates such as 2-amino-5-chlorophenol (68% activity), protocatechuate (33% activity) and catechol (5% activity). Both 2-aminophenol and 2-amino-5-cholorophenol are likely native substrates for this dioxygenase which is involved in the reductive degradation pathway of both nitrobenzene (NB) and 4-chloronitrobenzene (4-CNB), allowing C.testosteroni strain CNB-1 to grow on these compounds as sole source of carbon, nitrogen, and energy.<ref>PMID:15580337</ref> <ref>PMID:16517619</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 24:		Line 23:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Comamonas testosteroni]]	+	[[Category: Comamonas testosteroni CNB-1]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: Protocatechuate 4,5-dioxygenase]]~~	+	[[Category: Hou YJ]]
-	[[Category: Hou~~, Y J~~]]	+	[[Category: Hu Y]]
-	[[Category: Hu, Y]]	+	[[Category: Li DF]]
-	[[Category: Li~~, D F~~]]	+	[[Category: Liu W]]
-	[[Category: Liu, W]]	+	[[Category: Wang DC]]
-	[[Category: Wang~~, D C]]~~	+
-	~~[[Category: 2-his-1-carboxylate facial triad motif]]~~	+
-	~~[[Category: Cnbc]]~~	+
-	~~[[Category: Extradiol dioxygenase]]~~	+
-	~~[[Category: Oxidoreductase~~]]	+

OCA at 19:01, 27 July 2022

OCA — Wed, 27 Jul 2022 19:01:37 GMT

←Older revision		Revision as of 19:01, 27 July 2022
Line 1:		Line 1:

	==Crystal structure of native 1,6-APD (with Iron), 2-Animophenol-1,6-Dioxygenase==		==Crystal structure of native 1,6-APD (with Iron), 2-Animophenol-1,6-Dioxygenase==
-	<StructureSection load='3vsh' size='340' side='right' caption='[[3vsh]], [[Resolution\|resolution]] 2.70Å' scene=''>	+	<StructureSection load='3vsh' size='340' side='right'caption='[[3vsh]], [[Resolution\|resolution]] 2.70Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3vsh]] is a 4 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Comamonas_testosteroni Comamonas testosteroni]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VSH OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3VSH FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3vsh]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Comamonas_testosteroni Comamonas testosteroni]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VSH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VSH FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3vhg\|3vhg]], [[3vhi\|3vhi]], [[3vhj\|3vhj]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3vhg\|3vhg]], [[3vhi\|3vhi]], [[3vhj\|3vhj]]</div></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Protocatechuate_4,5-dioxygenase Protocatechuate 4,5-dioxygenase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.8 1.13.11.8] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Protocatechuate_4,5-dioxygenase Protocatechuate 4,5-dioxygenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.8 1.13.11.8] </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=3vsh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vsh OCA], [~~http~~://pdbe.org/3vsh PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3vsh RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3vsh PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3vsh 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=3vsh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vsh OCA], [https://pdbe.org/3vsh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vsh RCSB], [https://www.ebi.ac.uk/pdbsum/3vsh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vsh ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/AMNA_COMTE AMNA_COMTE]] Component of the 2-aminophenol 1,6-dioxygenase (APD) complex that catalyzes the ring fission of 2-aminophenol to produce 2-aminomuconic semialdehyde. CnbCa may have a role in the stability of the complex. The complex is also active on other substrates such as 2-amino-5-chlorophenol (68% activity), protocatechuate (33% activity) and catechol (5% activity). Both 2-aminophenol and 2-amino-5-cholorophenol are likely native substrates for this dioxygenase which is involved in the reductive degradation pathway of both nitrobenzene (NB) and 4-chloronitrobenzene (4-CNB), allowing C.testosteroni strain CNB-1 to grow on these compounds as sole source of carbon, nitrogen, and energy.<ref>PMID:15580337</ref> <ref>PMID:16517619</ref> [[~~http~~://www.uniprot.org/uniprot/AMNB_COMTE AMNB_COMTE]] Component of the 2-aminophenol 1,6-dioxygenase (APD) complex that catalyzes the ring fission of 2-aminophenol to produce 2-aminomuconic semialdehyde. CnbCb seems to be the catalytic subunit of the complex. Also active on other substrates such as 2-amino-5-chlorophenol (68% activity), protocatechuate (33% activity) and catechol (5% activity). Both 2-aminophenol and 2-amino-5-cholorophenol are likely native substrates for this dioxygenase which is involved in the reductive degradation pathway of both nitrobenzene (NB) and 4-chloronitrobenzene (4-CNB), allowing C.testosteroni strain CNB-1 to grow on these compounds as sole source of carbon, nitrogen, and energy.<ref>PMID:15580337</ref> <ref>PMID:16517619</ref>	+	[[https://www.uniprot.org/uniprot/AMNA_COMTE AMNA_COMTE]] Component of the 2-aminophenol 1,6-dioxygenase (APD) complex that catalyzes the ring fission of 2-aminophenol to produce 2-aminomuconic semialdehyde. CnbCa may have a role in the stability of the complex. The complex is also active on other substrates such as 2-amino-5-chlorophenol (68% activity), protocatechuate (33% activity) and catechol (5% activity). Both 2-aminophenol and 2-amino-5-cholorophenol are likely native substrates for this dioxygenase which is involved in the reductive degradation pathway of both nitrobenzene (NB) and 4-chloronitrobenzene (4-CNB), allowing C.testosteroni strain CNB-1 to grow on these compounds as sole source of carbon, nitrogen, and energy.<ref>PMID:15580337</ref> <ref>PMID:16517619</ref> [[https://www.uniprot.org/uniprot/AMNB_COMTE AMNB_COMTE]] Component of the 2-aminophenol 1,6-dioxygenase (APD) complex that catalyzes the ring fission of 2-aminophenol to produce 2-aminomuconic semialdehyde. CnbCb seems to be the catalytic subunit of the complex. Also active on other substrates such as 2-amino-5-chlorophenol (68% activity), protocatechuate (33% activity) and catechol (5% activity). Both 2-aminophenol and 2-amino-5-cholorophenol are likely native substrates for this dioxygenase which is involved in the reductive degradation pathway of both nitrobenzene (NB) and 4-chloronitrobenzene (4-CNB), allowing C.testosteroni strain CNB-1 to grow on these compounds as sole source of carbon, nitrogen, and energy.<ref>PMID:15580337</ref> <ref>PMID:16517619</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 25:		Line 25:
	</StructureSection>		</StructureSection>
	[[Category: Comamonas testosteroni]]		[[Category: Comamonas testosteroni]]
		+	[[Category: Large Structures]]
	[[Category: Protocatechuate 4,5-dioxygenase]]		[[Category: Protocatechuate 4,5-dioxygenase]]
	[[Category: Hou, Y J]]		[[Category: Hou, Y J]]

OCA at 08:34, 5 August 2016

OCA — Fri, 05 Aug 2016 08:34:29 GMT

←Older revision		Revision as of 08:34, 5 August 2016
Line 1:		Line 1:
		+
	==Crystal structure of native 1,6-APD (with Iron), 2-Animophenol-1,6-Dioxygenase==		==Crystal structure of native 1,6-APD (with Iron), 2-Animophenol-1,6-Dioxygenase==
	<StructureSection load='3vsh' size='340' side='right' caption='[[3vsh]], [[Resolution\|resolution]] 2.70Å' scene=''>		<StructureSection load='3vsh' size='340' side='right' caption='[[3vsh]], [[Resolution\|resolution]] 2.70Å' scene=''>
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3vhg\|3vhg]], [[3vhi\|3vhi]], [[3vhj\|3vhj]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3vhg\|3vhg]], [[3vhi\|3vhi]], [[3vhj\|3vhj]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protocatechuate_4,5-dioxygenase Protocatechuate 4,5-dioxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.8 1.13.11.8] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protocatechuate_4,5-dioxygenase Protocatechuate 4,5-dioxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.8 1.13.11.8] </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=3vsh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vsh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3vsh RCSB], [http://www.ebi.ac.uk/pdbsum/3vsh 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=3vsh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vsh OCA], [http://pdbe.org/3vsh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3vsh RCSB], [http://www.ebi.ac.uk/pdbsum/3vsh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3vsh ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[http://www.uniprot.org/uniprot/~~Q38M40_COMTE Q38M40_COMTE~~]] Component of the 2-aminophenol 1,6-dioxygenase (APD) complex that catalyzes the ring fission of 2-aminophenol to produce 2-aminomuconic semialdehyde. CnbCa may have a role in the stability of the complex. The complex is also active on other substrates such as 2-amino-5-chlorophenol (68% activity), protocatechuate (33% activity) and catechol (5% activity). Both 2-aminophenol and 2-amino-5-cholorophenol are likely native substrates for this dioxygenase which is involved in the reductive degradation pathway of both nitrobenzene (NB) and 4-chloronitrobenzene (4-CNB), allowing C.testosteroni strain CNB-1 to grow on these compounds as sole source of carbon, nitrogen, and energy.<ref>PMID:15580337</ref> <ref>PMID:16517619</ref> [[http://www.uniprot.org/uniprot/~~Q38M41_COMTE Q38M41_COMTE~~]] Component of the 2-aminophenol 1,6-dioxygenase (APD) complex that catalyzes the ring fission of 2-aminophenol to produce 2-aminomuconic semialdehyde. CnbCb seems to be the catalytic subunit of the complex. Also active on other substrates such as 2-amino-5-chlorophenol (68% activity), protocatechuate (33% activity) and catechol (5% activity). Both 2-aminophenol and 2-amino-5-cholorophenol are likely native substrates for this dioxygenase which is involved in the reductive degradation pathway of both nitrobenzene (NB) and 4-chloronitrobenzene (4-CNB), allowing C.testosteroni strain CNB-1 to grow on these compounds as sole source of carbon, nitrogen, and energy.<ref>PMID:15580337</ref> <ref>PMID:16517619</ref>	+	[[http://www.uniprot.org/uniprot/AMNA_COMTE AMNA_COMTE]] Component of the 2-aminophenol 1,6-dioxygenase (APD) complex that catalyzes the ring fission of 2-aminophenol to produce 2-aminomuconic semialdehyde. CnbCa may have a role in the stability of the complex. The complex is also active on other substrates such as 2-amino-5-chlorophenol (68% activity), protocatechuate (33% activity) and catechol (5% activity). Both 2-aminophenol and 2-amino-5-cholorophenol are likely native substrates for this dioxygenase which is involved in the reductive degradation pathway of both nitrobenzene (NB) and 4-chloronitrobenzene (4-CNB), allowing C.testosteroni strain CNB-1 to grow on these compounds as sole source of carbon, nitrogen, and energy.<ref>PMID:15580337</ref> <ref>PMID:16517619</ref> [[http://www.uniprot.org/uniprot/AMNB_COMTE AMNB_COMTE]] Component of the 2-aminophenol 1,6-dioxygenase (APD) complex that catalyzes the ring fission of 2-aminophenol to produce 2-aminomuconic semialdehyde. CnbCb seems to be the catalytic subunit of the complex. Also active on other substrates such as 2-amino-5-chlorophenol (68% activity), protocatechuate (33% activity) and catechol (5% activity). Both 2-aminophenol and 2-amino-5-cholorophenol are likely native substrates for this dioxygenase which is involved in the reductive degradation pathway of both nitrobenzene (NB) and 4-chloronitrobenzene (4-CNB), allowing C.testosteroni strain CNB-1 to grow on these compounds as sole source of carbon, nitrogen, and energy.<ref>PMID:15580337</ref> <ref>PMID:16517619</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 18:		Line 19:
	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 3vsh" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 00:48, 25 December 2014

OCA — Thu, 25 Dec 2014 00:48:08 GMT

←Older revision		Revision as of 00:48, 25 December 2014
Line 8:		Line 8:
	<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=3vsh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vsh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3vsh RCSB], [http://www.ebi.ac.uk/pdbsum/3vsh 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=3vsh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vsh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3vsh RCSB], [http://www.ebi.ac.uk/pdbsum/3vsh PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/Q38M40_COMTE Q38M40_COMTE]] Component of the 2-aminophenol 1,6-dioxygenase (APD) complex that catalyzes the ring fission of 2-aminophenol to produce 2-aminomuconic semialdehyde. CnbCa may have a role in the stability of the complex. The complex is also active on other substrates such as 2-amino-5-chlorophenol (68% activity), protocatechuate (33% activity) and catechol (5% activity). Both 2-aminophenol and 2-amino-5-cholorophenol are likely native substrates for this dioxygenase which is involved in the reductive degradation pathway of both nitrobenzene (NB) and 4-chloronitrobenzene (4-CNB), allowing C.testosteroni strain CNB-1 to grow on these compounds as sole source of carbon, nitrogen, and energy.<ref>PMID:15580337</ref> <ref>PMID:16517619</ref> [[http://www.uniprot.org/uniprot/Q38M41_COMTE Q38M41_COMTE]] Component of the 2-aminophenol 1,6-dioxygenase (APD) complex that catalyzes the ring fission of 2-aminophenol to produce 2-aminomuconic semialdehyde. CnbCb seems to be the catalytic subunit of the complex. Also active on other substrates such as 2-amino-5-chlorophenol (68% activity), protocatechuate (33% activity) and catechol (5% activity). Both 2-aminophenol and 2-amino-5-cholorophenol are likely native substrates for this dioxygenase which is involved in the reductive degradation pathway of both nitrobenzene (NB) and 4-chloronitrobenzene (4-CNB), allowing C.testosteroni strain CNB-1 to grow on these compounds as sole source of carbon, nitrogen, and energy.<ref>PMID:15580337</ref> <ref>PMID:16517619</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 15:29, 9 December 2014

OCA — Tue, 09 Dec 2014 15:29:32 GMT

←Older revision		Revision as of 15:29, 9 December 2014
Line 1:		Line 1:
-	[[~~Image:~~3vsh.~~jpg~~\|~~left~~\|~~200px~~]]	+	==Crystal structure of native 1,6-APD (with Iron), 2-Animophenol-1,6-Dioxygenase==
		+	<StructureSection load='3vsh' size='340' side='right' caption='[[3vsh]], [[Resolution\|resolution]] 2.70Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3vsh]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Comamonas_testosteroni Comamonas testosteroni]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VSH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3VSH FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3vhg\|3vhg]], [[3vhi\|3vhi]], [[3vhj\|3vhj]]</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protocatechuate_4,5-dioxygenase Protocatechuate 4,5-dioxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.8 1.13.11.8] </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=3vsh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vsh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3vsh RCSB], [http://www.ebi.ac.uk/pdbsum/3vsh PDBsum]</span></td></tr>
		+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Dioxygen activation by nonhaem Fe(II) enzymes containing the 2-His-1-carboxylate facial triad has been extensively studied in recent years. Here, crystal structures of 2-aminophenol 1,6-dioxygenase, an enzyme that represents a minor group of extradiol dioxygenases and that catalyses the ring opening of 2-aminophenol, in complex with the lactone intermediate (4Z,6Z)-3-iminooxepin-2(3H)-one and the product 2-aminomuconic 6-semialdehyde and in complex with the suicide inhibitor 4-nitrocatechol are reported. The Fe-ligand binding schemes observed in these structures revealed some common geometrical characteristics that are shared by the published structures of extradiol dioxygenases, suggesting that enzymes that catalyse the oxidation of noncatecholic compounds are very likely to utilize a similar strategy for dioxygen activation and the fission of aromatic rings as the canonical mechanism. The Fe-ligation arrangement, however, is strikingly enantiomeric to that of all other 2-His-1-carboxylate enzymes apart from protocatechuate 4,5-dioxygenase. This structural variance leads to the generation of an uncommon O(-)-Fe(2+)-O(-) species prior to O(2) binding, which probably forms the structural basis on which APD distinguishes its specific substrate and inhibitor, which share an analogous molecular structure.

-	~~{{STRUCTURE_3vsh\| PDB=3vsh \| SCENE= }}~~	+	Structures of aminophenol dioxygenase in complex with intermediate, product and inhibitor.,Li de F, Zhang JY, Hou YJ, Liu L, Hu Y, Liu SJ, Wang da C, Liu W Acta Crystallogr D Biol Crystallogr. 2013 Jan;69(Pt 1):32-43. doi:, 10.1107/S0907444912042072. Epub 2012 Dec 20. PMID:23275161<ref>PMID:23275161</ref>

-	~~===Crystal structure~~ of ~~native 1,6-APD (with Iron), 2-Animophenol-1,6-Dioxygenase===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_23275161}}~~	+	== References ==
-		+	<references/>
-	==~~About this Structure~~==	+	__TOC__
-	~~[[3vsh]] is a 4 chain structure with sequence from [http:~~//~~en.wikipedia.org/wiki/Comamonas_testosteroni Comamonas testosteroni]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VSH OCA].~~	+	</StructureSection>
	[[Category: Comamonas testosteroni]]		[[Category: Comamonas testosteroni]]
	[[Category: Protocatechuate 4,5-dioxygenase]]		[[Category: Protocatechuate 4,5-dioxygenase]]
-	[[Category: Hou, Y J.]]	+	[[Category: Hou, Y J]]
-	[[Category: Hu, Y.]]	+	[[Category: Hu, Y]]
-	[[Category: Li, D F.]]	+	[[Category: Li, D F]]
-	[[Category: Liu, W.]]	+	[[Category: Liu, W]]
-	[[Category: Wang, D C.]]	+	[[Category: Wang, D C]]
	[[Category: 2-his-1-carboxylate facial triad motif]]		[[Category: 2-his-1-carboxylate facial triad motif]]
	[[Category: Cnbc]]		[[Category: Cnbc]]
	[[Category: Extradiol dioxygenase]]		[[Category: Extradiol dioxygenase]]
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]

OCA at 08:44, 16 January 2013

OCA — Wed, 16 Jan 2013 08:44:11 GMT

←Older revision		Revision as of 08:44, 16 January 2013
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	[[Image:3vsh.jpg\|left\|200px]]

-	~~The entry~~ 3vsh ~~is ON HOLD~~ ~~until Paper Publication~~	+	{{STRUCTURE_3vsh\| PDB=3vsh \| SCENE= }}

-	~~Authors: Li~~, ~~D.F.~~, ~~Hou~~, ~~Y.J., Hu, Y., Wang, D.C., Liu, W.~~	+	===Crystal structure of native 1,6-APD (with Iron), 2-Animophenol-1,6-Dioxygenase===

-	~~Description: Crystal~~ structure ~~of native 1~~,6-~~APD (with Iron)~~, 2-~~Animophenol~~-1,6-~~Dioxygenase~~	+	{{ABSTRACT_PUBMED_23275161}}
		+
		+	==About this Structure==
		+	[[3vsh]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Comamonas_testosteroni Comamonas testosteroni]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VSH OCA].
		+	[[Category: Comamonas testosteroni]]
		+	[[Category: Protocatechuate 4,5-dioxygenase]]
		+	[[Category: Hou, Y J.]]
		+	[[Category: Hu, Y.]]
		+	[[Category: Li, D F.]]
		+	[[Category: Liu, W.]]
		+	[[Category: Wang, D C.]]
		+	[[Category: 2-his-1-carboxylate facial triad motif]]
		+	[[Category: Cnbc]]
		+	[[Category: Extradiol dioxygenase]]
		+	[[Category: Oxidoreductase]]

OCA at 07:08, 6 June 2012

OCA — Wed, 06 Jun 2012 07:08:50 GMT

←Older revision		Revision as of 07:08, 6 June 2012
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

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

	Authors: Li, D.F., Hou, Y.J., Hu, Y., Wang, D.C., Liu, W.		Authors: Li, D.F., Hou, Y.J., Hu, Y., Wang, D.C., Liu, W.

	Description: Crystal structure of native 1,6-APD (with Iron), 2-Animophenol-1,6-Dioxygenase		Description: Crystal structure of native 1,6-APD (with Iron), 2-Animophenol-1,6-Dioxygenase

OCA at 05:18, 30 May 2012

OCA — Wed, 30 May 2012 05:18:40 GMT

←Older revision		Revision as of 05:18, 30 May 2012
Line 5:		Line 5:
	Authors: Li, D.F., Hou, Y.J., Hu, Y., Wang, D.C., Liu, W.		Authors: Li, D.F., Hou, Y.J., Hu, Y., Wang, D.C., Liu, W.

-	Description: ~~CRYSTAL STRUCTURE OF NATIVE~~ 1,6-APD (~~WITH IRON~~), 2-~~ANIMOPHENOL~~-1,6-~~DIOXYGENASE~~	+	Description: Crystal structure of native 1,6-APD (with Iron), 2-Animophenol-1,6-Dioxygenase

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

OCA — Wed, 02 May 2012 18:47:11 GMT

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

←Older revision

Revision as of 18:47, 2 May 2012

OCA: New page: '''Unreleased structure''' The entry 3vsh is ON HOLD Authors: Li, D.F., Hou, Y.J., Hu, Y., Wang, D.C., Liu, W. Description: CRYSTAL STRUCTURE OF NATIVE 1,6-APD (WITH IRON), 2-ANIMOPHEN...

OCA — Wed, 02 May 2012 18:47:11 GMT

New page: '''Unreleased structure''' The entry 3vsh is ON HOLD Authors: Li, D.F., Hou, Y.J., Hu, Y., Wang, D.C., Liu, W. Description: CRYSTAL STRUCTURE OF NATIVE 1,6-APD (WITH IRON), 2-ANIMOPHEN...

New page

'''Unreleased structure'''

The entry 3vsh is ON HOLD

Authors: Li, D.F., Hou, Y.J., Hu, Y., Wang, D.C., Liu, W.

Description: CRYSTAL STRUCTURE OF NATIVE 1,6-APD (WITH IRON), 2-ANIMOPHENOL-1,6-DIOXYGENASE