1wor - Revision history

OCA at 13:33, 13 March 2024

2024-03-13T13:33:14Z

←Older revision		Revision as of 13:33, 13 March 2024
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	<StructureSection load='1wor' size='340' side='right'caption='[[1wor]], [[Resolution\|resolution]] 1.95Å' scene=''>		<StructureSection load='1wor' size='340' side='right'caption='[[1wor]], [[Resolution\|resolution]] 1.95Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1wor]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Atcc_43589 Atcc 43589~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WOR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WOR FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1wor]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WOR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WOR FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=RED:DIHYDROLIPOIC+ACID'>RED</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]] 1.95Å</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"~~><div style='overflow: auto; max-height: 3em;'>[[1woo\|1woo]], [[1wop\|1wop]], [[1wos\|1wos]]</div></td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=RED:DIHYDROLIPOIC+ACID'>RED</scene></td></tr>
-	~~<tr~~ id~~='activity'><td class~~="~~sblockLbl~~"><~~b>Activity:</b></td><td class~~=~~"sblockDat"><span class~~=~~'plainlinks~~'>~~[https://en.wikipedia.org/wiki/Aminomethyltransferase Aminomethyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.2.10 2.1.2.10]~~ </~~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=1wor FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wor OCA], [https://pdbe.org/1wor PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wor RCSB], [https://www.ebi.ac.uk/pdbsum/1wor PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wor 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=1wor FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wor OCA], [https://pdbe.org/1wor PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wor RCSB], [https://www.ebi.ac.uk/pdbsum/1wor PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wor ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/GCST_THEMA GCST_THEMA]] The glycine cleavage system catalyzes the degradation of glycine (By similarity).	+	[https://www.uniprot.org/uniprot/GCST_THEMA GCST_THEMA] The glycine cleavage system catalyzes the degradation of glycine (By similarity).
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 21:		Line 20:
	</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=1wor 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=1wor ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	The glycine cleavage system catalyzes the oxidative decarboxylation of glycine in bacteria and in mitochondria of animals and plants. Its deficiency in human causes nonketotic hyperglycinemia, an inborn error of glycine metabolism. T-protein, one of the four components of the glycine cleavage system,is a tetrahydrofolate dependent aminomethyltransferase. It catalyzes the transfer of the methylene carbon unit to tetrahydrofolate from the methylamine group covalently attached to the lipoamide arm of H-protein. To gain insight into the T-protein function at the molecular level, we have determined the first crystal structure of T-protein from Thermotoga maritima by the multiwavelength anomalous diffraction method of x-ray crystallography and refined four structures: the apoform; the tetrahydrofolate complex; the folinic acid complex; and the lipoic acid complex. The overall fold of T-protein is similar to that of the C-terminal tetrahydrofolate-binding region (residues 421-830) of Arthrobacter globiformis dimethylglycine oxidase. Tetrahydrofolate (or folinic acid) is bound near the center of the tripartite T-protein. Lipoic acid is bound adjacent to the tetrahydrofolate binding pocket, thus defining the interaction surface for H-protein binding. A homology model of the human T-protein provides the structural framework for understanding the molecular mechanisms underlying the development of nonketotic hyperglycinemia due to missense mutations of the human T-protein.
-
-	Crystal structure of T-protein of the glycine cleavage system. Cofactor binding, insights into H-protein recognition, and molecular basis for understanding nonketotic hyperglycinemia.,Lee HH, Kim DJ, Ahn HJ, Ha JY, Suh SW J Biol Chem. 2004 Nov 26;279(48):50514-23. Epub 2004 Sep 7. PMID:15355973<ref>PMID:15355973</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1wor" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Aminomethyltransferase 3D structures\|Aminomethyltransferase 3D structures]]		*[[Aminomethyltransferase 3D structures\|Aminomethyltransferase 3D structures]]
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Aminomethyltransferase]]
-	[[Category: Atcc 43589]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Ahn, H J~~]]	+	[[Category: Thermotoga maritima]]
-	[[Category: ~~Ha, J Y~~]]	+	[[Category: Ahn HJ]]
-	[[Category: ~~Kim, D J~~]]	+	[[Category: Ha JY]]
-	[[Category: ~~Lee, H H~~]]	+	[[Category: Kim DJ]]
-	[[Category: ~~Suh, S W~~]]	+	[[Category: Lee HH]]
-	[[Category: ~~Dihydrolipoic acid]]~~	+	[[Category: Suh SW]]
-	~~[[Category: T-protein]]~~	+
-	~~[[Category: Transferase~~]]	+

OCA at 16:23, 27 October 2021

2021-10-27T16:23:49Z

←Older revision		Revision as of 16:23, 27 October 2021
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	<StructureSection load='1wor' size='340' side='right'caption='[[1wor]], [[Resolution\|resolution]] 1.95Å' scene=''>		<StructureSection load='1wor' size='340' side='right'caption='[[1wor]], [[Resolution\|resolution]] 1.95Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1wor]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Atcc_43589 Atcc 43589]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WOR OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1WOR FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1wor]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_43589 Atcc 43589]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WOR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WOR FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=RED:DIHYDROLIPOIC+ACID'>RED</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=RED:DIHYDROLIPOIC+ACID'>RED</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1woo\|1woo]], [[1wop\|1wop]], [[1wos\|1wos]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1woo\|1woo]], [[1wop\|1wop]], [[1wos\|1wos]]</div></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Aminomethyltransferase Aminomethyltransferase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.2.10 2.1.2.10] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Aminomethyltransferase Aminomethyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.2.10 2.1.2.10] </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=1wor FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wor OCA], [~~http~~://pdbe.org/1wor PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1wor RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1wor PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1wor 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=1wor FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wor OCA], [https://pdbe.org/1wor PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wor RCSB], [https://www.ebi.ac.uk/pdbsum/1wor PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wor ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/GCST_THEMA GCST_THEMA]] The glycine cleavage system catalyzes the degradation of glycine (By similarity).	+	[[https://www.uniprot.org/uniprot/GCST_THEMA GCST_THEMA]] The glycine cleavage system catalyzes the degradation of glycine (By similarity).
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 17:19, 22 January 2020

2020-01-22T17:19:28Z

←Older revision		Revision as of 17:19, 22 January 2020
Line 1:		Line 1:

	==Crystal Structure of T-protein of the Glycine Cleavage System==		==Crystal Structure of T-protein of the Glycine Cleavage System==
-	<StructureSection load='1wor' size='340' side='right' caption='[[1wor]], [[Resolution\|resolution]] 1.95Å' scene=''>	+	<StructureSection load='1wor' size='340' side='right'caption='[[1wor]], [[Resolution\|resolution]] 1.95Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1wor]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43589 Atcc 43589]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WOR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1WOR FirstGlance]. <br>		<table><tr><td colspan='2'>[[1wor]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43589 Atcc 43589]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WOR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1WOR FirstGlance]. <br>
Line 32:		Line 32:

	==See Also==		==See Also==
-	*[[Aminomethyltransferase\|Aminomethyltransferase]]	+	*[[Aminomethyltransferase 3D structures\|Aminomethyltransferase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 39:		Line 39:
	[[Category: Aminomethyltransferase]]		[[Category: Aminomethyltransferase]]
	[[Category: Atcc 43589]]		[[Category: Atcc 43589]]
		+	[[Category: Large Structures]]
	[[Category: Ahn, H J]]		[[Category: Ahn, H J]]
	[[Category: Ha, J Y]]		[[Category: Ha, J Y]]

OCA at 16:05, 11 April 2018

2018-04-11T16:05:20Z

←Older revision		Revision as of 16:05, 11 April 2018
Line 1:		Line 1:
		+
	==Crystal Structure of T-protein of the Glycine Cleavage System==		==Crystal Structure of T-protein of the Glycine Cleavage System==
	<StructureSection load='1wor' size='340' side='right' caption='[[1wor]], [[Resolution\|resolution]] 1.95Å' scene=''>		<StructureSection load='1wor' size='340' side='right' caption='[[1wor]], [[Resolution\|resolution]] 1.95Å' scene=''>
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1woo\|1woo]], [[1wop\|1wop]], [[1wos\|1wos]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1woo\|1woo]], [[1wop\|1wop]], [[1wos\|1wos]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aminomethyltransferase Aminomethyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.2.10 2.1.2.10] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aminomethyltransferase Aminomethyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.2.10 2.1.2.10] </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=1wor FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wor OCA], [http://pdbe.org/1wor PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1wor RCSB], [http://www.ebi.ac.uk/pdbsum/1wor 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=1wor FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wor OCA], [http://pdbe.org/1wor PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1wor RCSB], [http://www.ebi.ac.uk/pdbsum/1wor PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1wor ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 14:		Line 15:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wo/1wor_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wo/1wor_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>

OCA at 06:22, 7 February 2016

2016-02-07T06:22:55Z

←Older revision		Revision as of 06:22, 7 February 2016
Line 18:		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=1wor ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 29:		Line 29:
	</div>		</div>
	<div class="pdbe-citations 1wor" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1wor" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Aminomethyltransferase\|Aminomethyltransferase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 22:41, 9 September 2015

2015-09-09T22:41:39Z

←Older revision		Revision as of 22:41, 9 September 2015
Line 2:		Line 2:
	<StructureSection load='1wor' size='340' side='right' caption='[[1wor]], [[Resolution\|resolution]] 1.95Å' scene=''>		<StructureSection load='1wor' size='340' side='right' caption='[[1wor]], [[Resolution\|resolution]] 1.95Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1wor]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Thermotoga_maritima Thermotoga maritima~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WOR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1WOR FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1wor]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43589 Atcc 43589]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WOR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1WOR FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=RED:DIHYDROLIPOIC+ACID'>RED</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=RED:DIHYDROLIPOIC+ACID'>RED</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1woo\|1woo]], [[1wop\|1wop]], [[1wos\|1wos]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1woo\|1woo]], [[1wop\|1wop]], [[1wos\|1wos]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aminomethyltransferase Aminomethyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.2.10 2.1.2.10] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aminomethyltransferase Aminomethyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.2.10 2.1.2.10] </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=1wor FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wor OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1wor RCSB], [http://www.ebi.ac.uk/pdbsum/1wor 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=1wor FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wor OCA], [http://pdbe.org/1wor PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1wor RCSB], [http://www.ebi.ac.uk/pdbsum/1wor PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 28:		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 1wor" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
Line 33:		Line 34:
	</StructureSection>		</StructureSection>
	[[Category: Aminomethyltransferase]]		[[Category: Aminomethyltransferase]]
-	[[Category: ~~Thermotoga maritima~~]]	+	[[Category: Atcc 43589]]
	[[Category: Ahn, H J]]		[[Category: Ahn, H J]]
	[[Category: Ha, J Y]]		[[Category: Ha, J Y]]

OCA at 08:35, 24 December 2014

2014-12-24T08:35:58Z

←Older revision		Revision as of 08:35, 24 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1wor]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WOR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1WOR FirstGlance]. <br>		<table><tr><td colspan='2'>[[1wor]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WOR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1WOR FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=RED:DIHYDROLIPOIC+ACID'>RED</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=RED:DIHYDROLIPOIC+ACID'>RED</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1woo\|1woo]], [[1wop\|1wop]], [[1wos\|1wos]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1woo\|1woo]], [[1wop\|1wop]], [[1wos\|1wos]]</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aminomethyltransferase Aminomethyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.2.10 2.1.2.10] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aminomethyltransferase Aminomethyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.2.10 2.1.2.10] </span></td></tr>
-	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1wor FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wor OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1wor RCSB], [http://www.ebi.ac.uk/pdbsum/1wor 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=1wor FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wor OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1wor RCSB], [http://www.ebi.ac.uk/pdbsum/1wor PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/GCST_THEMA GCST_THEMA]] The glycine cleavage system catalyzes the degradation of glycine (By similarity).
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 32:		Line 34:
	[[Category: Aminomethyltransferase]]		[[Category: Aminomethyltransferase]]
	[[Category: Thermotoga maritima]]		[[Category: Thermotoga maritima]]
-	[[Category: Ahn, H J.]]	+	[[Category: Ahn, H J]]
-	[[Category: Ha, J Y.]]	+	[[Category: Ha, J Y]]
-	[[Category: Kim, D J.]]	+	[[Category: Kim, D J]]
-	[[Category: Lee, H H.]]	+	[[Category: Lee, H H]]
-	[[Category: Suh, S W~~.]]~~	+	[[Category: Suh, S W]]
-	~~[[Category: Aminomethyltransferase~~]]	+
	[[Category: Dihydrolipoic acid]]		[[Category: Dihydrolipoic acid]]
	[[Category: T-protein]]		[[Category: T-protein]]
	[[Category: Transferase]]		[[Category: Transferase]]

OCA at 19:25, 29 September 2014

2014-09-29T19:25:50Z

←Older revision		Revision as of 19:25, 29 September 2014
Line 1:		Line 1:
-	[[~~Image:~~1wor.~~png~~\|~~left~~\|200px]]	+	==Crystal Structure of T-protein of the Glycine Cleavage System==
		+	<StructureSection load='1wor' size='340' side='right' caption='[[1wor]], [[Resolution\|resolution]] 1.95Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1wor]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WOR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1WOR FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=RED:DIHYDROLIPOIC+ACID'>RED</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1woo\|1woo]], [[1wop\|1wop]], [[1wos\|1wos]]</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aminomethyltransferase Aminomethyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.2.10 2.1.2.10] </span></td></tr>
		+	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1wor FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wor OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1wor RCSB], [http://www.ebi.ac.uk/pdbsum/1wor 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/wo/1wor_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 ==
		+	The glycine cleavage system catalyzes the oxidative decarboxylation of glycine in bacteria and in mitochondria of animals and plants. Its deficiency in human causes nonketotic hyperglycinemia, an inborn error of glycine metabolism. T-protein, one of the four components of the glycine cleavage system,is a tetrahydrofolate dependent aminomethyltransferase. It catalyzes the transfer of the methylene carbon unit to tetrahydrofolate from the methylamine group covalently attached to the lipoamide arm of H-protein. To gain insight into the T-protein function at the molecular level, we have determined the first crystal structure of T-protein from Thermotoga maritima by the multiwavelength anomalous diffraction method of x-ray crystallography and refined four structures: the apoform; the tetrahydrofolate complex; the folinic acid complex; and the lipoic acid complex. The overall fold of T-protein is similar to that of the C-terminal tetrahydrofolate-binding region (residues 421-830) of Arthrobacter globiformis dimethylglycine oxidase. Tetrahydrofolate (or folinic acid) is bound near the center of the tripartite T-protein. Lipoic acid is bound adjacent to the tetrahydrofolate binding pocket, thus defining the interaction surface for H-protein binding. A homology model of the human T-protein provides the structural framework for understanding the molecular mechanisms underlying the development of nonketotic hyperglycinemia due to missense mutations of the human T-protein.

-	~~{{STRUCTURE_1wor\| PDB=1wor \| SCENE= }}~~	+	Crystal structure of T-protein of the glycine cleavage system. Cofactor binding, insights into H-protein recognition, and molecular basis for understanding nonketotic hyperglycinemia.,Lee HH, Kim DJ, Ahn HJ, Ha JY, Suh SW J Biol Chem. 2004 Nov 26;279(48):50514-23. Epub 2004 Sep 7. PMID:15355973<ref>PMID:15355973</ref>

-	~~===Crystal Structure of T-protein~~ of the ~~Glycine Cleavage System===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_15355973}}~~	+	== References ==
-		+	<references/>
-	~~==About this Structure==~~	+	__TOC__
-	~~[[1wor]] is a 1 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Thermotoga_maritima Thermotoga maritima]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=1WOR OCA].~~	+	</StructureSection>
-		+
-	==~~Reference~~==	+
-	<~~ref group="xtra">PMID:015355973<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Aminomethyltransferase]]		[[Category: Aminomethyltransferase]]
	[[Category: Thermotoga maritima]]		[[Category: Thermotoga maritima]]

OCA: Protected "1wor" [edit=sysop:move=sysop]

2013-01-05T12:29:00Z

Protected "1wor" [edit=sysop:move=sysop]

←Older revision

Revision as of 12:29, 5 January 2013

OCA at 12:28, 5 January 2013

2013-01-05T12:28:58Z

←Older revision		Revision as of 12:28, 5 January 2013
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-	{{Seed}}
	[[Image:1wor.png\|left\|200px]]		[[Image:1wor.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_1wor", 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_1wor\| PDB=1wor \| SCENE= }}		{{STRUCTURE_1wor\| PDB=1wor \| SCENE= }}

	===Crystal Structure of T-protein of the Glycine Cleavage System===		===Crystal Structure of T-protein of the Glycine Cleavage System===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_15355973}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 15355973 is the PubMed ID number.
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	{{ABSTRACT_PUBMED_15355973}}		{{ABSTRACT_PUBMED_15355973}}

	==About this Structure==		==About this Structure==
-	~~1WOR~~ is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WOR OCA].	+	[[1wor]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WOR OCA].

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~15355973~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:015355973</ref><references group="xtra"/>
	[[Category: Aminomethyltransferase]]		[[Category: Aminomethyltransferase]]
	[[Category: Thermotoga maritima]]		[[Category: Thermotoga maritima]]
Line 34:		Line 22:
	[[Category: Dihydrolipoic acid]]		[[Category: Dihydrolipoic acid]]
	[[Category: T-protein]]		[[Category: T-protein]]
-		+	[[Category: Transferase]]
-	~~''Page seeded by~~ [~~http~~:~~//oca.weizmann.ac.il/oca OCA~~ ] ~~on Mon Feb 16 11:56:07 2009''~~	+