4add - Revision history

OCA at 07:14, 1 May 2024

2024-05-01T07:14:28Z

←Older revision		Revision as of 07:14, 1 May 2024
Line 3:		Line 3:
	<StructureSection load='4add' size='340' side='right'caption='[[4add]], [[Resolution\|resolution]] 2.45Å' scene=''>		<StructureSection load='4add' size='340' side='right'caption='[[4add]], [[Resolution\|resolution]] 2.45Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4add]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Escherichia_coli~~ Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ADD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ADD FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4add]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_BL21 Escherichia coli BL21]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ADD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ADD FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=PLP:PYRIDOXAL~~-~~5-PHOSPHATE'>PLP</scene>~~, ~~<scene name='pdbligand=SUO:N~~~2~~~-(3-CARBOXYPROPANOYL)-L-ORNITHINE'>SUO</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]] 2.45Å</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"><~~div style~~='~~overflow~~: ~~auto; max~~-~~height: 3em;~~'>~~[[4adb\|4adb]]~~, ~~[[4ade\|4ade]], [[4adc\|4adc]]~~</~~div~~></td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=SUO:N~2~-(3-CARBOXYPROPANOYL)-L-ORNITHINE'>SUO</scene></td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4add FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4add OCA], [https://pdbe.org/4add PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4add RCSB], [https://www.ebi.ac.uk/pdbsum/4add PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4add 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=4add FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4add OCA], [https://pdbe.org/4add PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4add RCSB], [https://www.ebi.ac.uk/pdbsum/4add PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4add ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/ASTC_ECOLI ASTC_ECOLI]] Catalyzes the transamination of N(2)-succinylornithine and alpha-ketoglutarate into N(2)-succinylglutamate semialdehyde and glutamate. Can also act as an acetylornithine aminotransferase.<ref>PMID:9696779</ref>	+	[https://www.uniprot.org/uniprot/ASTC_ECOLI ASTC_ECOLI] Catalyzes the transamination of N(2)-succinylornithine and alpha-ketoglutarate into N(2)-succinylglutamate semialdehyde and glutamate. Can also act as an acetylornithine aminotransferase.<ref>PMID:9696779</ref>
-	~~<div style="background-color:#fffaf0;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	possesses two acyl ornithine aminotransferases, one catabolic (AstC) and the other anabolic (ArgD), that participate in L-arginine metabolism. Although only 58% identical, the enzymes have been shown to be functionally interchangeable. Here we have purified AstC and have obtained X-ray crystal structures of apo and holo-AstC and of the enzyme complexed with its physiological substrate, succinylornithine. We compare the structures obtained in this study with those of ArgD from obtained elsewhere, finding several notable differences. Docking studies were used to explore the docking modes of several substrates (ornithine, succinylornithine and acetylornithine) and the co-substrate glutamate/alpha-ketogluterate. The docking studies support our observations that AstC has a strong preference for acylated ornithine species over ornithine itself, and suggest that the increase in specificity associated with acylation is caused by steric and desolvation effects rather than specific interactions between the substrate and enzyme.	+
-		+
-	Determination of the Structure of the Catabolic N-Succinylornithine Transaminase (AstC) from Escherichia coli.,Newman J, Seabrook S, Surjadi R, Williams CC, Lucent D, Wilding M, Scott C, Peat TS PLoS One. 2013;8(3):e58298. doi: 10.1371/journal.pone.0058298. Epub 2013 Mar 6. PMID:23484010<ref>PMID:23484010</ref>	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 4add" style="background-color:#fffaf0;"></div~~>	+

	==See Also==		==See Also==
Line 26:		Line 17:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Escherichia coli]]	+	[[Category: Escherichia coli BL21]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Newman, J]]	+	[[Category: Newman J]]
-	[[Category: Peat~~, T S]]~~	+	[[Category: Peat TS]]
-	~~[[Category: Aminotransferase]]~~	+
-	~~[[Category: Plp enzyme]]~~	+
-	~~[[Category: Transferase~~]]	+

OCA at 05:30, 25 August 2022

2022-08-25T05:30:25Z

←Older revision		Revision as of 05:30, 25 August 2022
Line 1:		Line 1:

	==Structural and functional study of succinyl-ornithine transaminase from E. coli==		==Structural and functional study of succinyl-ornithine transaminase from E. coli==
-	<StructureSection load='4add' size='340' side='right' caption='[[4add]], [[Resolution\|resolution]] 2.45Å' scene=''>	+	<StructureSection load='4add' size='340' side='right'caption='[[4add]], [[Resolution\|resolution]] 2.45Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4add]] is a 4 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ADD OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4ADD FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4add]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ADD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ADD FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=SUO:N~2~-(3-CARBOXYPROPANOYL)-L-ORNITHINE'>SUO</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=SUO:N~2~-(3-CARBOXYPROPANOYL)-L-ORNITHINE'>SUO</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4adb\|4adb]], [[4ade\|4ade]], [[4adc\|4adc]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[4adb\|4adb]], [[4ade\|4ade]], [[4adc\|4adc]]</div></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=4add FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4add OCA], [~~http~~://pdbe.org/4add PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4add RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4add PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4add 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=4add FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4add OCA], [https://pdbe.org/4add PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4add RCSB], [https://www.ebi.ac.uk/pdbsum/4add PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4add ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/ASTC_ECOLI ASTC_ECOLI]] Catalyzes the transamination of N(2)-succinylornithine and alpha-ketoglutarate into N(2)-succinylglutamate semialdehyde and glutamate. Can also act as an acetylornithine aminotransferase.<ref>PMID:9696779</ref>	+	[[https://www.uniprot.org/uniprot/ASTC_ECOLI ASTC_ECOLI]] Catalyzes the transamination of N(2)-succinylornithine and alpha-ketoglutarate into N(2)-succinylglutamate semialdehyde and glutamate. Can also act as an acetylornithine aminotransferase.<ref>PMID:9696779</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 21:		Line 21:

	==See Also==		==See Also==
-	*[[Aminotransferase\|Aminotransferase]]	+	*[[Aminotransferase 3D structures\|Aminotransferase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 27:		Line 27:
	</StructureSection>		</StructureSection>
	[[Category: Escherichia coli]]		[[Category: Escherichia coli]]
		+	[[Category: Large Structures]]
	[[Category: Newman, J]]		[[Category: Newman, J]]
	[[Category: Peat, T S]]		[[Category: Peat, T S]]

OCA at 08:02, 6 March 2019

2019-03-06T08:02:49Z

←Older revision		Revision as of 08:02, 6 March 2019
Line 1:		Line 1:

	==Structural and functional study of succinyl-ornithine transaminase from E. coli==		==Structural and functional study of succinyl-ornithine transaminase from E. coli==
-	<StructureSection load='4add' size='340' side='right' caption='[[4add]], [[Resolution\|resolution]] 2.45Å' scene=''>	+	<StructureSection load='4add' size='340' side='right' caption='[[4add]], [[Resolution\|resolution]] 2.45Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4add]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ADD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ADD FirstGlance]. <br>		<table><tr><td colspan='2'>[[4add]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ADD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ADD FirstGlance]. <br>

OCA at 02:21, 5 August 2016

2016-08-05T02:21:37Z

←Older revision		Revision as of 02:21, 5 August 2016
Line 1:		Line 1:
		+
	==Structural and functional study of succinyl-ornithine transaminase from E. coli==		==Structural and functional study of succinyl-ornithine transaminase from E. coli==
	<StructureSection load='4add' size='340' side='right' caption='[[4add]], [[Resolution\|resolution]] 2.45Å' scene=''>		<StructureSection load='4add' size='340' side='right' caption='[[4add]], [[Resolution\|resolution]] 2.45Å' scene=''>
Line 5:		Line 6:
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=SUO:N~2~-(3-CARBOXYPROPANOYL)-L-ORNITHINE'>SUO</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=SUO:N~2~-(3-CARBOXYPROPANOYL)-L-ORNITHINE'>SUO</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4adb\|4adb]], [[4ade\|4ade]], [[4adc\|4adc]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4adb\|4adb]], [[4ade\|4ade]], [[4adc\|4adc]]</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=4add FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4add OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4add RCSB], [http://www.ebi.ac.uk/pdbsum/4add 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=4add FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4add OCA], [http://pdbe.org/4add PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4add RCSB], [http://www.ebi.ac.uk/pdbsum/4add PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4add ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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 4add" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Aminotransferase\|Aminotransferase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 15:03, 25 December 2014

2014-12-25T15:03:57Z

←Older revision		Revision as of 15:03, 25 December 2014
Line 7:		Line 7:
	<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=4add FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4add OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4add RCSB], [http://www.ebi.ac.uk/pdbsum/4add 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=4add FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4add OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4add RCSB], [http://www.ebi.ac.uk/pdbsum/4add PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/ASTC_ECOLI ASTC_ECOLI]] Catalyzes the transamination of N(2)-succinylornithine and alpha-ketoglutarate into N(2)-succinylglutamate semialdehyde and glutamate. Can also act as an acetylornithine aminotransferase.<ref>PMID:9696779</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 10:02, 21 December 2014

2014-12-21T10:02:27Z

←Older revision		Revision as of 10:02, 21 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_4add\| PDB=4add \| SCENE= }}~~	+	==Structural and functional study of succinyl-ornithine transaminase from E. coli==
-	===Structural and functional study of succinyl-ornithine transaminase from E. coli===	+	<StructureSection load='4add' size='340' side='right' caption='[[4add]], [[Resolution\|resolution]] 2.45Å' scene=''>
-	~~{{ABSTRACT_PUBMED_23484010}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4add]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ADD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ADD FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=SUO:N~2~-(3-CARBOXYPROPANOYL)-L-ORNITHINE'>SUO</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4adb\|4adb]], [[4ade\|4ade]], [[4adc\|4adc]]</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=4add FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4add OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4add RCSB], [http://www.ebi.ac.uk/pdbsum/4add PDBsum]</span></td></tr>
		+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	possesses two acyl ornithine aminotransferases, one catabolic (AstC) and the other anabolic (ArgD), that participate in L-arginine metabolism. Although only 58% identical, the enzymes have been shown to be functionally interchangeable. Here we have purified AstC and have obtained X-ray crystal structures of apo and holo-AstC and of the enzyme complexed with its physiological substrate, succinylornithine. We compare the structures obtained in this study with those of ArgD from obtained elsewhere, finding several notable differences. Docking studies were used to explore the docking modes of several substrates (ornithine, succinylornithine and acetylornithine) and the co-substrate glutamate/alpha-ketogluterate. The docking studies support our observations that AstC has a strong preference for acylated ornithine species over ornithine itself, and suggest that the increase in specificity associated with acylation is caused by steric and desolvation effects rather than specific interactions between the substrate and enzyme.

-	~~==Function==~~	+	Determination of the Structure of the Catabolic N-Succinylornithine Transaminase (AstC) from Escherichia coli.,Newman J, Seabrook S, Surjadi R, Williams CC, Lucent D, Wilding M, Scott C, Peat TS PLoS One. 2013;8(3):e58298. doi: 10.1371/journal.pone.0058298. Epub 2013 Mar 6. PMID:23484010<ref>PMID:23484010</ref>
-	~~[[http://www.uniprot.org/uniprot/ASTC_ECOLI ASTC_ECOLI]] Catalyzes~~ the ~~transamination~~ of N(2)~~-succinylornithine and alpha-ketoglutarate into N~~(2)~~-succinylglutamate semialdehyde and glutamate~~. ~~Can also act as an acetylornithine aminotransferase~~.<ref>PMID:~~9696779~~</ref>	+

-	~~==About this Structure==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[4add]] is~~ a ~~4 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Escherichia_coli Escherichia coli]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=4ADD OCA].~~	+	</div>
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Escherichia coli]]		[[Category: Escherichia coli]]
-	[[Category: Newman, J.]]	+	[[Category: Newman, J]]
-	[[Category: Peat, T S.]]	+	[[Category: Peat, T S]]
	[[Category: Aminotransferase]]		[[Category: Aminotransferase]]
	[[Category: Plp enzyme]]		[[Category: Plp enzyme]]
	[[Category: Transferase]]		[[Category: Transferase]]

OCA at 07:41, 27 March 2013

2013-03-27T07:41:36Z

←Older revision		Revision as of 07:41, 27 March 2013
Line 1:		Line 1:
-	[[Image:4add.jpg\|left\|200px]]
-
	{{STRUCTURE_4add\| PDB=4add \| SCENE= }}		{{STRUCTURE_4add\| PDB=4add \| SCENE= }}
-
	===Structural and functional study of succinyl-ornithine transaminase from E. coli===		===Structural and functional study of succinyl-ornithine transaminase from E. coli===
		+	{{ABSTRACT_PUBMED_23484010}}

		+	==Function==
		+	[[http://www.uniprot.org/uniprot/ASTC_ECOLI ASTC_ECOLI]] Catalyzes the transamination of N(2)-succinylornithine and alpha-ketoglutarate into N(2)-succinylglutamate semialdehyde and glutamate. Can also act as an acetylornithine aminotransferase.<ref>PMID:9696779</ref>

	==About this Structure==		==About this Structure==
	[[4add]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ADD OCA].		[[4add]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ADD OCA].
		+
		+	==Reference==
		+	<references group="xtra"/><references/>
	[[Category: Escherichia coli]]		[[Category: Escherichia coli]]
	[[Category: Newman, J.]]		[[Category: Newman, J.]]

OCA at 09:06, 16 January 2013

2013-01-16T09:06:37Z

←Older revision		Revision as of 09:06, 16 January 2013
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	[[Image:4add.jpg\|left\|200px]]

-	~~The entry~~ 4add ~~is ON HOLD~~ ~~until Paper Publication~~	+	{{STRUCTURE_4add\| PDB=4add \| SCENE= }}

-	~~Authors: Newman, J., Peat, T.S~~.	+	===Structural and functional study of succinyl-ornithine transaminase from E. coli===

-	~~Description~~: ~~Structural and functional study of succinyl-ornithine transaminase~~ from E. coli	+
		+	==About this Structure==
		+	[[4add]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ADD OCA].
		+	[[Category: Escherichia coli]]
		+	[[Category: Newman, J.]]
		+	[[Category: Peat, T S.]]
		+	[[Category: Aminotransferase]]
		+	[[Category: Plp enzyme]]
		+	[[Category: Transferase]]

OCA at 06:07, 8 February 2012

2012-02-08T06:07:59Z

←Older revision		Revision as of 06:07, 8 February 2012
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

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

	Authors: Newman, J., Peat, T.S.		Authors: Newman, J., Peat, T.S.

	Description: Structural and functional study of succinyl-ornithine transaminase from E. coli		Description: Structural and functional study of succinyl-ornithine transaminase from E. coli

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

2012-01-04T05:51:15Z

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

←Older revision

Revision as of 05:51, 4 January 2012