3wgc - Revision history

OCA at 08:45, 20 March 2024

OCA — Wed, 20 Mar 2024 08:45:06 GMT

←Older revision		Revision as of 08:45, 20 March 2024
Line 3:		Line 3:
	<StructureSection load='3wgc' size='340' side='right'caption='[[3wgc]], [[Resolution\|resolution]] 2.50Å' scene=''>		<StructureSection load='3wgc' size='340' side='right'caption='[[3wgc]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3wgc]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Aerja Aerja~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WGC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WGC FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3wgc]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Aeromonas_jandaei Aeromonas jandaei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WGC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WGC FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=PLG:N-GLYCINE~~-[~~3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YL-METHANE]'>PLG</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]] 2.5Å</td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>~~[~~[Related_structure~~\|~~Related:~~]]~~</b></td><td class="sblockDat"><div style='overflow: auto~~; ~~max-height: 3em;'>[[3wgb\|3wgb]]</div>~~</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PLG:N-GLYCINE-[3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YL-METHANE]'>PLG</scene></td></tr>
-	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat"~~>LATA, ltaA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&~~id~~=650 AERJA])</td></tr>~~	+
-	~~<tr id='activity'><td class~~="~~sblockLbl~~"><~~b>Activity:</b></td><td class~~=~~"sblockDat"><span class~~=~~'plainlinks'>[https~~:~~//en.wikipedia.org/wiki/L~~-~~allo~~-~~threonine_aldolase L~~-~~allo~~-~~threonine aldolase], with EC number [https://www.brenda~~-~~enzymes.info/php/result_flat.php4?ecno=~~4~~.1.2.49 4.1.2.49~~] </~~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=3wgc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wgc OCA], [https://pdbe.org/3wgc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wgc RCSB], [https://www.ebi.ac.uk/pdbsum/3wgc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wgc 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=3wgc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wgc OCA], [https://pdbe.org/3wgc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wgc RCSB], [https://www.ebi.ac.uk/pdbsum/3wgc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wgc ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/LTAA_AERJA LTAA_AERJA]] Stereospecifically catalyzes the interconversion of L-allo-threonine and glycine.	+	[https://www.uniprot.org/uniprot/LTAA_AERJA LTAA_AERJA] Stereospecifically catalyzes the interconversion of L-allo-threonine and glycine.
-	~~<div style="background-color:#fffaf0;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	L-allo-Threonine aldolase (LATA), a pyridoxal-5'-phosphate-dependent enzyme from Aeromonas jandaei DK-39, stereospecifically catalyzes the reversible interconversion of L-allo-threonine to glycine and acetaldehyde. Here, the crystal structures of LATA and its mutant LATA_H128Y/S292R were determined at 2.59 and 2.50 A resolution, respectively. Their structures implied that conformational changes in the loop consisting of residues Ala123-Pro131, where His128 moved 4.2 A outwards from the active site on mutation to a tyrosine residue, regulate the substrate specificity for L-allo-threonine versus L-threonine. Saturation mutagenesis of His128 led to diverse stereoselectivity towards L-allo-threonine and L-threonine. Moreover, the H128Y mutant showed the highest activity towards the two substrates, with an 8.4-fold increase towards L-threonine and a 2.0-fold increase towards L-allo-threonine compared with the wild-type enzyme. The crystal structures of LATA and its mutant LATA_H128Y/S292R reported here will provide further insights into the regulation of the stereoselectivity of threonine aldolases targeted for the catalysis of L-allo-threonine/L-threonine synthesis.	+
-		+
-	L-allo-Threonine aldolase with an H128Y/S292R mutation from Aeromonas jandaei DK-39 reveals the structural basis of changes in substrate stereoselectivity.,Qin HM, Imai FL, Miyakawa T, Kataoka M, Kitamura N, Urano N, Mori K, Kawabata H, Okai M, Ohtsuka J, Hou F, Nagata K, Shimizu S, Tanokura M Acta Crystallogr D Biol Crystallogr. 2014 Jun;70(Pt 6):1695-703. doi:, 10.1107/S1399004714007664. Epub 2014 May 30. PMID:24914980<ref>PMID:24914980</ref>	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 3wgc" style="background-color:#fffaf0;"></div>~~	+

	==See Also==		==See Also==
	*[[Aldolase 3D structures\|Aldolase 3D structures]]		*[[Aldolase 3D structures\|Aldolase 3D structures]]
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Aerja]]~~	+	[[Category: Aeromonas jandaei]]
-	~~[[Category: L-allo-threonine aldolase~~]]	+
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Hou, F]]	+	[[Category: Hou F]]
-	[[Category: Imai~~, F L~~]]	+	[[Category: Imai FL]]
-	[[Category: Kataoka, M]]	+	[[Category: Kataoka M]]
-	[[Category: Miyakawa, T]]	+	[[Category: Miyakawa T]]
-	[[Category: Nagata, K]]	+	[[Category: Nagata K]]
-	[[Category: Ohtsuka, J]]	+	[[Category: Ohtsuka J]]
-	[[Category: Okai, M]]	+	[[Category: Okai M]]
-	[[Category: Qin~~, H M~~]]	+	[[Category: Qin HM]]
-	[[Category: Shimizu, S]]	+	[[Category: Shimizu S]]
-	[[Category: Tanokura, M]]	+	[[Category: Tanokura M]]
-	~~[[Category: Lyase]]~~	+
-	~~[[Category: Pyridoxal-5'-phosphate]]~~	+
-	~~[[Category: Threonine aldolase~~]]	+

OCA at 05:35, 3 August 2022

OCA — Wed, 03 Aug 2022 05:35:29 GMT

←Older revision		Revision as of 05:35, 3 August 2022
Line 1:		Line 1:

	==Aeromonas jandaei L-allo-threonine aldolase H128Y/S292R double mutant==		==Aeromonas jandaei L-allo-threonine aldolase H128Y/S292R double mutant==
-	<StructureSection load='3wgc' size='340' side='right' caption='[[3wgc]], [[Resolution\|resolution]] 2.50Å' scene=''>	+	<StructureSection load='3wgc' size='340' side='right'caption='[[3wgc]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3wgc]] is a 4 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Aerja Aerja]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WGC OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3WGC FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3wgc]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Aerja Aerja]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WGC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WGC FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PLG:N-GLYCINE-[3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YL-METHANE]'>PLG</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PLG:N-GLYCINE-[3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YL-METHANE]'>PLG</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3wgb\|3wgb]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3wgb\|3wgb]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">LATA, ltaA ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=650 AERJA])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">LATA, ltaA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=650 AERJA])</td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/L-allo-threonine_aldolase L-allo-threonine aldolase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.49 4.1.2.49] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/L-allo-threonine_aldolase L-allo-threonine aldolase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.49 4.1.2.49] </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=3wgc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wgc OCA], [~~http~~://pdbe.org/3wgc PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3wgc RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3wgc PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3wgc 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=3wgc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wgc OCA], [https://pdbe.org/3wgc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wgc RCSB], [https://www.ebi.ac.uk/pdbsum/3wgc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wgc ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/LTAA_AERJA LTAA_AERJA]] Stereospecifically catalyzes the interconversion of L-allo-threonine and glycine.	+	[[https://www.uniprot.org/uniprot/LTAA_AERJA LTAA_AERJA]] Stereospecifically catalyzes the interconversion of L-allo-threonine and glycine.
	<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==
-	*[[Aldolase\|Aldolase]]	+	*[[Aldolase 3D structures\|Aldolase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 30:		Line 30:
	[[Category: Aerja]]		[[Category: Aerja]]
	[[Category: L-allo-threonine aldolase]]		[[Category: L-allo-threonine aldolase]]
		+	[[Category: Large Structures]]
	[[Category: Hou, F]]		[[Category: Hou, F]]
	[[Category: Imai, F L]]		[[Category: Imai, F L]]

OCA at 09:11, 21 February 2019

OCA — Thu, 21 Feb 2019 09:11:46 GMT

←Older revision		Revision as of 09:11, 21 February 2019
Line 3:		Line 3:
	<StructureSection load='3wgc' size='340' side='right' caption='[[3wgc]], [[Resolution\|resolution]] 2.50Å' scene=''>		<StructureSection load='3wgc' size='340' side='right' caption='[[3wgc]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3wgc]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WGC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WGC FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3wgc]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Aerja Aerja]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WGC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WGC FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PLG:N-GLYCINE-[3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YL-METHANE]'>PLG</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PLG:N-GLYCINE-[3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YL-METHANE]'>PLG</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3wgb\|3wgb]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3wgb\|3wgb]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">LATA, ltaA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=650 AERJA])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/L-allo-threonine_aldolase L-allo-threonine aldolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.49 4.1.2.49] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/L-allo-threonine_aldolase L-allo-threonine aldolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.49 4.1.2.49] </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=3wgc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wgc OCA], [http://pdbe.org/3wgc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3wgc RCSB], [http://www.ebi.ac.uk/pdbsum/3wgc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3wgc ProSAT]</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=3wgc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wgc OCA], [http://pdbe.org/3wgc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3wgc RCSB], [http://www.ebi.ac.uk/pdbsum/3wgc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3wgc ProSAT]</span></td></tr>
Line 27:		Line 28:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Aerja]]
	[[Category: L-allo-threonine aldolase]]		[[Category: L-allo-threonine aldolase]]
	[[Category: Hou, F]]		[[Category: Hou, F]]

OCA at 10:54, 5 August 2016

OCA — Fri, 05 Aug 2016 10:54:45 GMT

←Older revision		Revision as of 10:54, 5 August 2016
Line 1:		Line 1:
		+
	==Aeromonas jandaei L-allo-threonine aldolase H128Y/S292R double mutant==		==Aeromonas jandaei L-allo-threonine aldolase H128Y/S292R double mutant==
	<StructureSection load='3wgc' size='340' side='right' caption='[[3wgc]], [[Resolution\|resolution]] 2.50Å' scene=''>		<StructureSection load='3wgc' size='340' side='right' caption='[[3wgc]], [[Resolution\|resolution]] 2.50Å' scene=''>
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3wgb\|3wgb]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3wgb\|3wgb]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/L-allo-threonine_aldolase L-allo-threonine aldolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.49 4.1.2.49] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/L-allo-threonine_aldolase L-allo-threonine aldolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.49 4.1.2.49] </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=3wgc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wgc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3wgc RCSB], [http://www.ebi.ac.uk/pdbsum/3wgc 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=3wgc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wgc OCA], [http://pdbe.org/3wgc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3wgc RCSB], [http://www.ebi.ac.uk/pdbsum/3wgc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3wgc ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 18:		Line 19:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 3wgc" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Aldolase\|Aldolase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 18:12, 25 December 2014

OCA — Thu, 25 Dec 2014 18:12:31 GMT

←Older revision		Revision as of 18:12, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3wgc]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WGC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WGC FirstGlance]. <br>		<table><tr><td colspan='2'>[[3wgc]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WGC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WGC FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PLG:N-GLYCINE-[3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YL-METHANE]'>PLG</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PLG:N-GLYCINE-[3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YL-METHANE]'>PLG</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3wgb\|3wgb]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3wgb\|3wgb]]</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/L-allo-threonine_aldolase L-allo-threonine aldolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.49 4.1.2.49] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/L-allo-threonine_aldolase L-allo-threonine aldolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.49 4.1.2.49] </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=3wgc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wgc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3wgc RCSB], [http://www.ebi.ac.uk/pdbsum/3wgc 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=3wgc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wgc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3wgc RCSB], [http://www.ebi.ac.uk/pdbsum/3wgc PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/LTAA_AERJA LTAA_AERJA]] Stereospecifically catalyzes the interconversion of L-allo-threonine and glycine.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 21:		Line 23:
	</StructureSection>		</StructureSection>
	[[Category: L-allo-threonine aldolase]]		[[Category: L-allo-threonine aldolase]]
-	[[Category: Hou, F.]]	+	[[Category: Hou, F]]
-	[[Category: Imai, F L.]]	+	[[Category: Imai, F L]]
-	[[Category: Kataoka, M.]]	+	[[Category: Kataoka, M]]
-	[[Category: Miyakawa, T.]]	+	[[Category: Miyakawa, T]]
-	[[Category: Nagata, K.]]	+	[[Category: Nagata, K]]
-	[[Category: Ohtsuka, J.]]	+	[[Category: Ohtsuka, J]]
-	[[Category: Okai, M.]]	+	[[Category: Okai, M]]
-	[[Category: Qin, H M.]]	+	[[Category: Qin, H M]]
-	[[Category: Shimizu, S.]]	+	[[Category: Shimizu, S]]
-	[[Category: Tanokura, M.]]	+	[[Category: Tanokura, M]]
	[[Category: Lyase]]		[[Category: Lyase]]
	[[Category: Pyridoxal-5'-phosphate]]		[[Category: Pyridoxal-5'-phosphate]]
	[[Category: Threonine aldolase]]		[[Category: Threonine aldolase]]

OCA at 07:21, 9 July 2014

OCA — Wed, 09 Jul 2014 07:21:33 GMT

←Older revision		Revision as of 07:21, 9 July 2014
Line 1:		Line 1:
-	'''~~Unreleased~~ structure'''	+	==Aeromonas jandaei L-allo-threonine aldolase H128Y/S292R double mutant==
		+	<StructureSection load='3wgc' size='340' side='right' caption='[[3wgc]], [[Resolution\|resolution]] 2.50Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3wgc]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WGC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WGC FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PLG:N-GLYCINE-[3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YL-METHANE]'>PLG</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3wgb\|3wgb]]</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/L-allo-threonine_aldolase L-allo-threonine aldolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.49 4.1.2.49] </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=3wgc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wgc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3wgc RCSB], [http://www.ebi.ac.uk/pdbsum/3wgc PDBsum]</span></td></tr>
		+	<table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	L-allo-Threonine aldolase (LATA), a pyridoxal-5'-phosphate-dependent enzyme from Aeromonas jandaei DK-39, stereospecifically catalyzes the reversible interconversion of L-allo-threonine to glycine and acetaldehyde. Here, the crystal structures of LATA and its mutant LATA_H128Y/S292R were determined at 2.59 and 2.50 A resolution, respectively. Their structures implied that conformational changes in the loop consisting of residues Ala123-Pro131, where His128 moved 4.2 A outwards from the active site on mutation to a tyrosine residue, regulate the substrate specificity for L-allo-threonine versus L-threonine. Saturation mutagenesis of His128 led to diverse stereoselectivity towards L-allo-threonine and L-threonine. Moreover, the H128Y mutant showed the highest activity towards the two substrates, with an 8.4-fold increase towards L-threonine and a 2.0-fold increase towards L-allo-threonine compared with the wild-type enzyme. The crystal structures of LATA and its mutant LATA_H128Y/S292R reported here will provide further insights into the regulation of the stereoselectivity of threonine aldolases targeted for the catalysis of L-allo-threonine/L-threonine synthesis.

-	~~The entry 3wgc is ON HOLD until Paper Publication~~	+	L-allo-Threonine aldolase with an H128Y/S292R mutation from Aeromonas jandaei DK-39 reveals the structural basis of changes in substrate stereoselectivity.,Qin HM, Imai FL, Miyakawa T, Kataoka M, Kitamura N, Urano N, Mori K, Kawabata H, Okai M, Ohtsuka J, Hou F, Nagata K, Shimizu S, Tanokura M Acta Crystallogr D Biol Crystallogr. 2014 Jun;70(Pt 6):1695-703. doi:, 10.1107/S1399004714007664. Epub 2014 May 30. PMID:24914980<ref>PMID:24914980</ref>

-	~~Authors: Qin~~, H.-M., Imai, F.L.~~, Miyakawa, T.,~~ Kataoka, M., ~~Okai, M~~., Ohtsuka, J., ~~Hou, F~~., ~~Nagata, K~~., Shimizu, S., Tanokura, M.	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~Description~~: ~~Aeromonas jandaei L~~-~~allo~~-~~threonine~~ aldolase ~~H128Y/S292R double mutant~~	+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: L-allo-threonine aldolase]]
		+	[[Category: Hou, F.]]
		+	[[Category: Imai, F L.]]
		+	[[Category: Kataoka, M.]]
		+	[[Category: Miyakawa, T.]]
		+	[[Category: Nagata, K.]]
		+	[[Category: Ohtsuka, J.]]
		+	[[Category: Okai, M.]]
		+	[[Category: Qin, H M.]]
		+	[[Category: Shimizu, S.]]
		+	[[Category: Tanokura, M.]]
		+	[[Category: Lyase]]
		+	[[Category: Pyridoxal-5'-phosphate]]
		+	[[Category: Threonine aldolase]]

OCA at 08:18, 26 March 2014

OCA — Wed, 26 Mar 2014 08:18:50 GMT

←Older revision		Revision as of 08:18, 26 March 2014
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

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

	Authors: Qin, H.-M., Imai, F.L., Miyakawa, T., Kataoka, M., Okai, M., Ohtsuka, J., Hou, F., Nagata, K., Shimizu, S., Tanokura, M.		Authors: Qin, H.-M., Imai, F.L., Miyakawa, T., Kataoka, M., Okai, M., Ohtsuka, J., Hou, F., Nagata, K., Shimizu, S., Tanokura, M.

	Description: Aeromonas jandaei L-allo-threonine aldolase H128Y/S292R double mutant		Description: Aeromonas jandaei L-allo-threonine aldolase H128Y/S292R double mutant

OCA at 06:16, 28 August 2013

OCA — Wed, 28 Aug 2013 06:16:41 GMT

←Older revision		Revision as of 06:16, 28 August 2013
Line 3:		Line 3:
	The entry 3wgc is ON HOLD		The entry 3wgc is ON HOLD

-	Authors: Qin, H.-M., Imai, F.L., Miyakawa, T. , Kataoka, M., Okai, M. , Ohtsuka, J. , Hou, F. , Nagata, K. , Shimizu, S. , Tanokura, M.	+	Authors: Qin, H.-M., Imai, F.L., Miyakawa, T., Kataoka, M., Okai, M., Ohtsuka, J., Hou, F., Nagata, K., Shimizu, S., Tanokura, M.

-	Description: ~~AEROMONAS JANDAEI~~ L-~~ALLO~~-~~THREONINE ALDOLASE~~ H128Y/S292R ~~DOUBLE MUTANT~~	+	Description: Aeromonas jandaei L-allo-threonine aldolase H128Y/S292R double mutant

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

OCA — Wed, 14 Aug 2013 06:54:39 GMT

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

←Older revision

Revision as of 06:54, 14 August 2013

OCA: New page: '''Unreleased structure''' The entry 3wgc is ON HOLD Authors: Qin, H.-M., Imai, F.L., Miyakawa, T. , Kataoka, M., Okai, M. , Ohtsuka, J. , Hou, F. , Nagata, K. , Shimizu, S. , Tanokura,...

OCA — Wed, 14 Aug 2013 06:54:37 GMT

New page: '''Unreleased structure''' The entry 3wgc is ON HOLD Authors: Qin, H.-M., Imai, F.L., Miyakawa, T. , Kataoka, M., Okai, M. , Ohtsuka, J. , Hou, F. , Nagata, K. , Shimizu, S. , Tanokura,...

New page

'''Unreleased structure'''

The entry 3wgc is ON HOLD

Authors: Qin, H.-M., Imai, F.L., Miyakawa, T. , Kataoka, M., Okai, M. , Ohtsuka, J. , Hou, F. , Nagata, K. , Shimizu, S. , Tanokura, M.

Description: AEROMONAS JANDAEI L-ALLO-THREONINE ALDOLASE H128Y/S292R DOUBLE MUTANT