3r5e - Revision history

OCA at 12:10, 14 March 2024

OCA — Thu, 14 Mar 2024 12:10:49 GMT

←Older revision		Revision as of 12:10, 14 March 2024
Line 3:		Line 3:
	<StructureSection load='3r5e' size='340' side='right'caption='[[3r5e]], [[Resolution\|resolution]] 2.10Å' scene=''>		<StructureSection load='3r5e' size='340' side='right'caption='[[3r5e]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3r5e]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~"micrococcus_glutamicus"_kinoshita_et_al._1958 "micrococcus glutamicus" kinoshita et al. 1958~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3R5E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3R5E FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3r5e]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Corynebacterium_glutamicum Corynebacterium glutamicum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3R5E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3R5E FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.1Å</td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>~~[[~~Related_structure~~\|~~Related:~~]]~~</b></td><td class="sblockDat"><div style='overflow: auto~~; ~~max-height: 3em;'>[[3r8r\|3r8r]]</div>~~</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat"~~>cg1776, Cgl1575, tal ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&~~id=~~1718~~ "~~Micrococcus glutamicus~~" ~~Kinoshita et al. 1958])</td~~><~~/tr>~~	+
-	~~<tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b></td><td class="sblockDat"><span class='plainlinks~~'>~~[https://en.wikipedia.org/wiki/Transaldolase Transaldolase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.2.1.2 2.2.1.2]~~ </~~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=3r5e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3r5e OCA], [https://pdbe.org/3r5e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3r5e RCSB], [https://www.ebi.ac.uk/pdbsum/3r5e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3r5e 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=3r5e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3r5e OCA], [https://pdbe.org/3r5e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3r5e RCSB], [https://www.ebi.ac.uk/pdbsum/3r5e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3r5e ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/Q8NQ64_CORGL Q8NQ64_CORGL]] Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway (By similarity).[HAMAP-Rule:MF_00493]	+	[https://www.uniprot.org/uniprot/Q8NQ64_CORGL Q8NQ64_CORGL] Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway (By similarity).[HAMAP-Rule:MF_00493]
-	~~<div style="background-color:#fffaf0;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	Transaldolase (Tal) is involved in the central carbon metabolism, i.e. the non-oxidative pentose phosphate pathway, and is therefore a ubiquitous enzyme. However, Tals show a low degree in sequence identity and vary in length within the enzyme family which previously led to the definition of five subfamilies. We wondered how this variation is conserved in structure and function. To answer this question we characterised and compared the Tals from Bacillus subtilis, Corynebacterium glutamicum and Escherichia coli, each belonging to a different subfamily, with respect to their biochemical properties and structures. The overall structure of the Tal domain, a (beta/alpha)(8) -barrel fold, is well conserved between the different subfamilies but the enzymes show different degrees of oligomerisation (monomer, dimer and decamer). The substrate specificity of the three enzymes investigated is quite similar which is reflected in the conservation of the active site, the phosphate binding site as well as the position of a catalytically important water molecule. All decameric enzymes characterised so far appear to be heat stable no matter whether they originate from a mesophilic or thermophilic organism. Hence, the thermostability might be due to the structural properties, i.e. tight packing, of these enzymes. Database The crystal structures have been deposited in the Protein Data Bank with accession code 3R8R for BsTal and 3R5E for CgTal. Structured digital abstract * BsTal and BsTal bind by x-ray crystallography (View interaction) * BsTal and BsTal bind by x-ray crystallography (View interaction).	+
-		+
-	Conservation of structure and mechanism within the transaldolase enzyme family.,Samland AK, Baier S, Schurmann M, Inoue T, Huf S, Schneider G, Sprenger GA, Sandalova T FEBS J. 2011 Dec 25. doi: 10.1111/j.1742-4658.2011.08467.x. PMID:22212631<ref>PMID:22212631</ref>	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 3r5e" style="background-color:#fffaf0;"></div>~~	+

	==See Also==		==See Also==
	*[[Transaldolase 3D structures\|Transaldolase 3D structures]]		*[[Transaldolase 3D structures\|Transaldolase 3D structures]]
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Micrococcus glutamicus kinoshita et al. 1958~~]]	+	[[Category: Corynebacterium glutamicum]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: Transaldolase]]~~	+	[[Category: Samland AK]]
-	[[Category: Samland~~, A K~~]]	+	[[Category: Sandalova T]]
-	[[Category: Sandalova, T]]	+	[[Category: Schneider G]]
-	[[Category: Schneider, G]]	+
-	~~[[Category: Pentose phosphate pathway]]~~	+
-	~~[[Category: Tim barrel fold]]~~	+
-	~~[[Category: Transferase~~]]	+

OCA at 05:49, 15 June 2022

OCA — Wed, 15 Jun 2022 05:49:36 GMT

←Older revision		Revision as of 05:49, 15 June 2022
Line 1:		Line 1:

	==TRANSALDOLASE from Corynebacterium glutamicum==		==TRANSALDOLASE from Corynebacterium glutamicum==
-	<StructureSection load='3r5e' size='340' side='right' caption='[[3r5e]], [[Resolution\|resolution]] 2.10Å' scene=''>	+	<StructureSection load='3r5e' size='340' side='right'caption='[[3r5e]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3r5e]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/"micrococcus_glutamicus"_kinoshita_et_al._1958 "micrococcus glutamicus" kinoshita et al. 1958]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3R5E OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3R5E FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3r5e]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"micrococcus_glutamicus"_kinoshita_et_al._1958 "micrococcus glutamicus" kinoshita et al. 1958]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3R5E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3R5E FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3r8r\|3r8r]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3r8r\|3r8r]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">cg1776, Cgl1575, tal ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1718 "Micrococcus glutamicus" Kinoshita et al. 1958])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">cg1776, Cgl1575, tal ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1718 "Micrococcus glutamicus" Kinoshita et al. 1958])</td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Transaldolase Transaldolase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.2.1.2 2.2.1.2] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Transaldolase Transaldolase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.2.1.2 2.2.1.2] </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=3r5e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3r5e OCA], [~~http~~://pdbe.org/3r5e PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3r5e RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3r5e PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3r5e 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=3r5e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3r5e OCA], [https://pdbe.org/3r5e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3r5e RCSB], [https://www.ebi.ac.uk/pdbsum/3r5e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3r5e ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/Q8NQ64_CORGL Q8NQ64_CORGL]] Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway (By similarity).[HAMAP-Rule:MF_00493]	+	[[https://www.uniprot.org/uniprot/Q8NQ64_CORGL Q8NQ64_CORGL]] Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway (By similarity).[HAMAP-Rule:MF_00493]
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 23:		Line 23:

	==See Also==		==See Also==
-	*[[Transaldolase\|Transaldolase]]	+	*[[Transaldolase 3D structures\|Transaldolase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 29:		Line 29:
	</StructureSection>		</StructureSection>
	[[Category: Micrococcus glutamicus kinoshita et al. 1958]]		[[Category: Micrococcus glutamicus kinoshita et al. 1958]]
		+	[[Category: Large Structures]]
	[[Category: Transaldolase]]		[[Category: Transaldolase]]
	[[Category: Samland, A K]]		[[Category: Samland, A K]]

OCA at 04:24, 5 August 2016

OCA — Fri, 05 Aug 2016 04:24:56 GMT

←Older revision		Revision as of 04:24, 5 August 2016
Line 1:		Line 1:
		+
	==TRANSALDOLASE from Corynebacterium glutamicum==		==TRANSALDOLASE from Corynebacterium glutamicum==
	<StructureSection load='3r5e' size='340' side='right' caption='[[3r5e]], [[Resolution\|resolution]] 2.10Å' scene=''>		<StructureSection load='3r5e' size='340' side='right' caption='[[3r5e]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3r5e]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Corynebacterium_glutamicum Corynebacterium glutamicum~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3R5E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3R5E FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3r5e]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"micrococcus_glutamicus"_kinoshita_et_al._1958 "micrococcus glutamicus" kinoshita et al. 1958]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3R5E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3R5E FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3r8r\|3r8r]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3r8r\|3r8r]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">cg1776, Cgl1575, tal ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1718 ~~Corynebacterium glutamicum~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">cg1776, Cgl1575, tal ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1718 "Micrococcus glutamicus" Kinoshita et al. 1958])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Transaldolase Transaldolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.2.1.2 2.2.1.2] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Transaldolase Transaldolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.2.1.2 2.2.1.2] </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=3r5e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3r5e OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3r5e RCSB], [http://www.ebi.ac.uk/pdbsum/3r5e 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=3r5e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3r5e OCA], [http://pdbe.org/3r5e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3r5e RCSB], [http://www.ebi.ac.uk/pdbsum/3r5e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3r5e ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 19:		Line 20:
	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 3r5e" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 26:		Line 28:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Corynebacterium glutamicum~~]]	+	[[Category: Micrococcus glutamicus kinoshita et al. 1958]]
	[[Category: Transaldolase]]		[[Category: Transaldolase]]
	[[Category: Samland, A K]]		[[Category: Samland, A K]]

OCA at 15:47, 25 December 2014

OCA — Thu, 25 Dec 2014 15:47:53 GMT

←Older revision		Revision as of 15:47, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3r5e]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Corynebacterium_glutamicum Corynebacterium glutamicum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3R5E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3R5E FirstGlance]. <br>		<table><tr><td colspan='2'>[[3r5e]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Corynebacterium_glutamicum Corynebacterium glutamicum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3R5E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3R5E FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3r8r\|3r8r]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3r8r\|3r8r]]</td></tr>
-	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">cg1776, Cgl1575, tal ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1718 Corynebacterium glutamicum])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">cg1776, Cgl1575, tal ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1718 Corynebacterium glutamicum])</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Transaldolase Transaldolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.2.1.2 2.2.1.2] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Transaldolase Transaldolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.2.1.2 2.2.1.2] </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=3r5e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3r5e OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3r5e RCSB], [http://www.ebi.ac.uk/pdbsum/3r5e 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=3r5e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3r5e OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3r5e RCSB], [http://www.ebi.ac.uk/pdbsum/3r5e PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/Q8NQ64_CORGL Q8NQ64_CORGL]] Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway (By similarity).[HAMAP-Rule:MF_00493]
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 15:		Line 17:
	Conservation of structure and mechanism within the transaldolase enzyme family.,Samland AK, Baier S, Schurmann M, Inoue T, Huf S, Schneider G, Sprenger GA, Sandalova T FEBS J. 2011 Dec 25. doi: 10.1111/j.1742-4658.2011.08467.x. PMID:22212631<ref>PMID:22212631</ref>		Conservation of structure and mechanism within the transaldolase enzyme family.,Samland AK, Baier S, Schurmann M, Inoue T, Huf S, Schneider G, Sprenger GA, Sandalova T FEBS J. 2011 Dec 25. doi: 10.1111/j.1742-4658.2011.08467.x. PMID:22212631<ref>PMID:22212631</ref>

-	From ~~MEDLINEÂ®~~/~~PubMedÂ®~~, 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>

Line 26:		Line 28:
	[[Category: Corynebacterium glutamicum]]		[[Category: Corynebacterium glutamicum]]
	[[Category: Transaldolase]]		[[Category: Transaldolase]]
-	[[Category: Samland, A K.]]	+	[[Category: Samland, A K]]
-	[[Category: Sandalova, T.]]	+	[[Category: Sandalova, T]]
-	[[Category: Schneider, G.]]	+	[[Category: Schneider, G]]
	[[Category: Pentose phosphate pathway]]		[[Category: Pentose phosphate pathway]]
	[[Category: Tim barrel fold]]		[[Category: Tim barrel fold]]
-	[[Category: Transaldolase]]
	[[Category: Transferase]]		[[Category: Transferase]]

OCA at 04:53, 5 June 2014

OCA — Thu, 05 Jun 2014 04:53:14 GMT

←Older revision		Revision as of 04:53, 5 June 2014
Line 1:		Line 1:
-	[[~~Image:~~3r5e.~~png~~\|~~left~~\|~~200px~~]]	+	==TRANSALDOLASE from Corynebacterium glutamicum==
		+	<StructureSection load='3r5e' size='340' side='right' caption='[[3r5e]], [[Resolution\|resolution]] 2.10Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3r5e]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Corynebacterium_glutamicum Corynebacterium glutamicum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3R5E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3R5E FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3r8r\|3r8r]]</td></tr>
		+	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">cg1776, Cgl1575, tal ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1718 Corynebacterium glutamicum])</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Transaldolase Transaldolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.2.1.2 2.2.1.2] </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=3r5e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3r5e OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3r5e RCSB], [http://www.ebi.ac.uk/pdbsum/3r5e PDBsum]</span></td></tr>
		+	<table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Transaldolase (Tal) is involved in the central carbon metabolism, i.e. the non-oxidative pentose phosphate pathway, and is therefore a ubiquitous enzyme. However, Tals show a low degree in sequence identity and vary in length within the enzyme family which previously led to the definition of five subfamilies. We wondered how this variation is conserved in structure and function. To answer this question we characterised and compared the Tals from Bacillus subtilis, Corynebacterium glutamicum and Escherichia coli, each belonging to a different subfamily, with respect to their biochemical properties and structures. The overall structure of the Tal domain, a (beta/alpha)(8) -barrel fold, is well conserved between the different subfamilies but the enzymes show different degrees of oligomerisation (monomer, dimer and decamer). The substrate specificity of the three enzymes investigated is quite similar which is reflected in the conservation of the active site, the phosphate binding site as well as the position of a catalytically important water molecule. All decameric enzymes characterised so far appear to be heat stable no matter whether they originate from a mesophilic or thermophilic organism. Hence, the thermostability might be due to the structural properties, i.e. tight packing, of these enzymes. Database The crystal structures have been deposited in the Protein Data Bank with accession code 3R8R for BsTal and 3R5E for CgTal. Structured digital abstract * BsTal and BsTal bind by x-ray crystallography (View interaction) * BsTal and BsTal bind by x-ray crystallography (View interaction).

-	~~<!--~~	+	Conservation of structure and mechanism within the transaldolase enzyme family.,Samland AK, Baier S, Schurmann M, Inoue T, Huf S, Schneider G, Sprenger GA, Sandalova T FEBS J. 2011 Dec 25. doi: 10.1111/j.1742-4658.2011.08467.x. PMID:22212631<ref>PMID:22212631</ref>
-	~~The line below this paragraph, containing "STRUCTURE_3r5e", 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_3r5e\| PDB=3r5e \| SCENE= }}~~	+

-	~~===TRANSALDOLASE from Corynebacterium glutamicum===~~	+	From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>
		+	</div>

-		+	==See Also==
-	~~<!--~~	+	*[[Transaldolase\|Transaldolase]]
-	~~The line below this paragraph, {{ABSTRACT_PUBMED_22212631}}, adds the Publication Abstract to the page~~	+	== References ==
-	~~(as it appears on PubMed at http://www.pubmed.gov), where 22212631 is the PubMed ID number.~~	+	<references/>
-	~~-->~~	+	__TOC__
-	~~{{ABSTRACT_PUBMED_22212631}}~~	+	</StructureSection>
-		+
-	==~~About this Structure~~==	+
-	[[~~3r5e~~]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Corynebacterium_glutamicum Corynebacterium glutamicum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3R5E OCA].	+
-		+
-	==~~Reference~~==	+
-	<~~ref group="xtra">PMID:022212631<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Corynebacterium glutamicum]]		[[Category: Corynebacterium glutamicum]]
	[[Category: Transaldolase]]		[[Category: Transaldolase]]

OCA at 06:43, 21 March 2012

OCA — Wed, 21 Mar 2012 06:43:21 GMT

←Older revision		Revision as of 06:43, 21 March 2012
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-	[[Image:3r5e.~~jpg~~\|left\|200px]]	+	[[Image:3r5e.png\|left\|200px]]

	<!--		<!--

OCA at 06:30, 8 February 2012

OCA — Wed, 08 Feb 2012 06:30:47 GMT

←Older revision		Revision as of 06:30, 8 February 2012
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	[[Image:3r5e.jpg\|left\|200px]]

-	The ~~entry 3r5e~~ is ~~ON HOLD~~ ~~until Paper Publication~~	+	<!--
		+	The line below this paragraph, containing "STRUCTURE_3r5e", 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_3r5e\| PDB=3r5e \| SCENE= }}

-	~~Authors: Sandalova, T., Samland, A.K., Schneider, G.~~	+	===TRANSALDOLASE from Corynebacterium glutamicum===

-	~~Description~~: ~~TRANSALDOLASE~~ from Corynebacterium glutamicum	+
		+	<!--
		+	The line below this paragraph, {{ABSTRACT_PUBMED_22212631}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 22212631 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_22212631}}
		+
		+	==About this Structure==
		+	[[3r5e]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Corynebacterium_glutamicum Corynebacterium glutamicum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3R5E OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:022212631</ref><references group="xtra"/>
		+	[[Category: Corynebacterium glutamicum]]
		+	[[Category: Transaldolase]]
		+	[[Category: Samland, A K.]]
		+	[[Category: Sandalova, T.]]
		+	[[Category: Schneider, G.]]
		+	[[Category: Pentose phosphate pathway]]
		+	[[Category: Tim barrel fold]]
		+	[[Category: Transaldolase]]
		+	[[Category: Transferase]]

OCA at 05:11, 18 May 2011

OCA — Wed, 18 May 2011 05:11:40 GMT

←Older revision		Revision as of 05:11, 18 May 2011
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 3r5e is ON HOLD	+	The entry 3r5e is ON HOLD until Paper Publication

	Authors: Sandalova, T., Samland, A.K., Schneider, G.		Authors: Sandalova, T., Samland, A.K., Schneider, G.

	Description: TRANSALDOLASE from Corynebacterium glutamicum		Description: TRANSALDOLASE from Corynebacterium glutamicum

OCA: Protected "3r5e" [edit=sysop:move=sysop]

OCA — Wed, 30 Mar 2011 07:48:42 GMT

Protected "3r5e" [edit=sysop:move=sysop]

←Older revision

Revision as of 07:48, 30 March 2011

OCA: New page: '''Unreleased structure''' The entry 3r5e is ON HOLD Authors: Sandalova, T., Samland, A.K., Schneider, G. Description: TRANSALDOLASE from Corynebacterium glutamicum

OCA — Wed, 30 Mar 2011 07:48:41 GMT

New page: '''Unreleased structure''' The entry 3r5e is ON HOLD Authors: Sandalova, T., Samland, A.K., Schneider, G. Description: TRANSALDOLASE from Corynebacterium glutamicum

New page

'''Unreleased structure'''

The entry 3r5e is ON HOLD

Authors: Sandalova, T., Samland, A.K., Schneider, G.

Description: TRANSALDOLASE from Corynebacterium glutamicum