3vsg - Revision history

OCA at 08:41, 20 March 2024

2024-03-20T08:41:42Z

← Older revision		Revision as of 08:41, 20 March 2024
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	<StructureSection load='3vsg' size='340' side='right'caption='[[3vsg]], [[Resolution\|resolution]] 2.40Å' scene=''>		<StructureSection load='3vsg' size='340' side='right'caption='[[3vsg]], [[Resolution\|resolution]] 2.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3vsg]] 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=3VSG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VSG FirstGlance]. <br>		<table><tr><td colspan='2'>[[3vsg]] 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=3VSG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VSG FirstGlance]. <br>
	</td></tr><tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat">~~<div style='overflow: auto; max~~-~~height: 3em;'>[[3vsh\|3vsh]]~~, [[~~3vsi~~\|~~3vsi~~]]~~, [[3vsj\|3vsj]]</div></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='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=3vsg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vsg OCA], [https://pdbe.org/3vsg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vsg RCSB], [https://www.ebi.ac.uk/pdbsum/3vsg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vsg 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=3vsg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vsg OCA], [https://pdbe.org/3vsg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vsg RCSB], [https://www.ebi.ac.uk/pdbsum/3vsg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vsg 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;">~~
	~~== 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.

	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>

	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~
	~~</div>~~
	~~<div class="pdbe-citations 3vsg" style="background-color:#fffaf0;"></div~~>
	== References ==		== References ==
	<references/>		<references/>
	__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

2022-07-27T19:01:34Z

← Older revision		Revision as of 19:01, 27 July 2022
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	==Crystal structure of iron free 1,6-APD, 2-Animophenol-1,6-Dioxygenase==		==Crystal structure of iron free 1,6-APD, 2-Animophenol-1,6-Dioxygenase==
	<StructureSection load='3vsg' size='340' side='right' caption='[[3vsg]], [[Resolution\|resolution]] 2.40Å' scene=''>		<StructureSection load='3vsg' size='340' side='right'caption='[[3vsg]], [[Resolution\|resolution]] 2.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3vsg]] 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=3VSG OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3VSG FirstGlance]. <br>		<table><tr><td colspan='2'>[[3vsg]] 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=3VSG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VSG FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3vsh\|3vsh]], [[3vsi\|3vsi]], [[3vsj\|3vsj]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3vsh\|3vsh]], [[3vsi\|3vsi]], [[3vsj\|3vsj]]</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=3vsg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vsg OCA], [~~http~~://pdbe.org/3vsg PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3vsg RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3vsg PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3vsg 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=3vsg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vsg OCA], [https://pdbe.org/3vsg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vsg RCSB], [https://www.ebi.ac.uk/pdbsum/3vsg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vsg 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 ==
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	</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 21:45, 4 August 2016

2016-08-04T21:45:22Z

← Older revision		Revision as of 21:45, 4 August 2016
Line 1:		Line 1:

	==Crystal structure of iron free 1,6-APD, 2-Animophenol-1,6-Dioxygenase==		==Crystal structure of iron free 1,6-APD, 2-Animophenol-1,6-Dioxygenase==
	<StructureSection load='3vsg' size='340' side='right' caption='[[3vsg]], [[Resolution\|resolution]] 2.40Å' scene=''>		<StructureSection load='3vsg' size='340' side='right' caption='[[3vsg]], [[Resolution\|resolution]] 2.40Å' scene=''>
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	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3vsh\|3vsh]], [[3vsi\|3vsi]], [[3vsj\|3vsj]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3vsh\|3vsh]], [[3vsi\|3vsi]], [[3vsj\|3vsj]]</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=3vsg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vsg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3vsg RCSB], [http://www.ebi.ac.uk/pdbsum/3vsg 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=3vsg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vsg OCA], [http://pdbe.org/3vsg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3vsg RCSB], [http://www.ebi.ac.uk/pdbsum/3vsg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3vsg 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 17:		Line 18:
	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 3vsg" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 19:56, 24 December 2014

2014-12-24T19:56:16Z

← Older revision		Revision as of 19:56, 24 December 2014
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	<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=3vsg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vsg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3vsg RCSB], [http://www.ebi.ac.uk/pdbsum/3vsg 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=3vsg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vsg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3vsg RCSB], [http://www.ebi.ac.uk/pdbsum/3vsg 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 15:17, 9 December 2014

2014-12-09T15:17:59Z

← Older revision		Revision as of 15:17, 9 December 2014
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	[[~~Image~~:~~3vsg~~.~~jpg~~\|~~left~~\|~~200px~~]]		==Crystal structure of iron free 1,6-APD, 2-Animophenol-1,6-Dioxygenase==
			<StructureSection load='3vsg' size='340' side='right' caption='[[3vsg]], [[Resolution\|resolution]] 2.40Å' scene=''>
			== Structural highlights ==
			<table><tr><td colspan='2'>[[3vsg]] 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=3VSG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3VSG FirstGlance]. <br>
			</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3vsh\|3vsh]], [[3vsi\|3vsi]], [[3vsj\|3vsj]]</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=3vsg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vsg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3vsg RCSB], [http://www.ebi.ac.uk/pdbsum/3vsg 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_3vsg\| PDB=3vsg \| 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 ~~iron free 1,6-APD, 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__
	~~[[3vsg]] 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=3VSG 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 08:58, 16 January 2013

2013-01-16T08:58:04Z

← Older revision		Revision as of 08:58, 16 January 2013
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	~~'''Unreleased structure'''~~		[[Image:3vsg.jpg\|left\|200px]]

	~~The entry~~ 3vsg ~~is ON HOLD~~ ~~until Paper Publication~~		{{STRUCTURE_3vsg\| PDB=3vsg \| SCENE= }}

	~~Authors: Li~~, ~~D.F.~~, ~~Hou~~, ~~Y.J., Hu, Y., Wang, D.C., Liu, W.~~		===Crystal structure of iron free 1,6-APD, 2-Animophenol-1,6-Dioxygenase===

	~~Description~~: ~~Crystal structure of iron free 1~~,6-~~APD~~, 2-~~Animophenol~~-1,6-~~Dioxygenase~~		{{ABSTRACT_PUBMED_23275161}}

			==About this Structure==
			[[3vsg]] 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=3VSG 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

2012-06-06T07:08:49Z

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

	The entry 3vsg is ON HOLD		The entry 3vsg 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 iron free 1,6-APD, 2-Animophenol-1,6-Dioxygenase		Description: Crystal structure of iron free 1,6-APD, 2-Animophenol-1,6-Dioxygenase

OCA at 05:18, 30 May 2012

2012-05-30T05:18:38Z

← Older revision		Revision as of 05:18, 30 May 2012
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	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 IRON FREE~~ 1,6-APD, 2-~~ANIMOPHENOL~~-1,6-~~DIOXYGENASE~~		Description: Crystal structure of iron free 1,6-APD, 2-Animophenol-1,6-Dioxygenase

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

2012-05-02T18:47:10Z

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

← Older revision	Revision as of 18:47, 2 May 2012
(No difference)

OCA: New page: '''Unreleased structure''' The entry 3vsg is ON HOLD Authors: Li, D.F., Hou, Y.J., Hu, Y., Wang, D.C., Liu, W. Description: CRYSTAL STRUCTURE OF IRON FREE 1,6-APD, 2-ANIMOPHENOL-1,6-DI...

2012-05-02T18:47:09Z

New page: '''Unreleased structure''' The entry 3vsg is ON HOLD Authors: Li, D.F., Hou, Y.J., Hu, Y., Wang, D.C., Liu, W. Description: CRYSTAL STRUCTURE OF IRON FREE 1,6-APD, 2-ANIMOPHENOL-1,6-DI...

New page

'''Unreleased structure'''

The entry 3vsg is ON HOLD

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

Description: CRYSTAL STRUCTURE OF IRON FREE 1,6-APD, 2-ANIMOPHENOL-1,6-DIOXYGENASE