4dpp - Revision history

OCA at 08:48, 20 March 2024

2024-03-20T08:48:48Z

← Older revision		Revision as of 08:48, 20 March 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4dpp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DPP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DPP FirstGlance]. <br>		<table><tr><td colspan='2'>[[4dpp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DPP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DPP FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</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]] 2Å</td></tr>
			<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</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=4dpp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dpp OCA], [https://pdbe.org/4dpp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dpp RCSB], [https://www.ebi.ac.uk/pdbsum/4dpp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dpp 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=4dpp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dpp OCA], [https://pdbe.org/4dpp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dpp RCSB], [https://www.ebi.ac.uk/pdbsum/4dpp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dpp ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[https://www.uniprot.org/uniprot/DAPA2_ARATH DAPA2_ARATH]] Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA) (By similarity).		[https://www.uniprot.org/uniprot/DAPA2_ARATH DAPA2_ARATH] Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA) (By similarity).
	~~<div style="background-color:#fffaf0;">~~
	~~== Publication Abstract from PubMed ==~~
	In plants, the lysine biosynthetic pathway is an attractive target for both the development of herbicides and increasing the nutritional value of crops given that lysine is a limiting amino acid in cereals. Dihydrodipicolinate synthase (DHDPS) and dihydrodipicolinate reductase (DHDPR) catalyse the first two committed steps of lysine biosynthesis. Here, we carry out for the first time a comprehensive characterisation of the structure and activity of both DHDPS and DHDPR from Arabidopsis thaliana. The A. thaliana DHDPS enzyme (At-DHDPS2) has similar activity to the bacterial form of the enzyme, but is more strongly allosterically inhibited by (S)-lysine. Structural studies of At-DHDPS2 show (S)-lysine bound at a cleft between two monomers, highlighting the allosteric site; however, unlike previous studies, binding is not accompanied by conformational changes, suggesting that binding may cause changes in protein dynamics rather than large conformation changes. DHDPR from A. thaliana (At-DHDPR2) has similar specificity for both NADH and NADPH during catalysis, and has tighter binding of substrate than has previously been reported. While all known bacterial DHDPR enzymes have a tetrameric structure, analytical ultracentrifugation, and scattering data unequivocally show that At-DHDPR2 exists as a dimer in solution. The exact arrangement of the dimeric protein is as yet unknown, but ab initio modelling of x-ray scattering data is consistent with an elongated structure in solution, which does not correspond to any of the possible dimeric pairings observed in the X-ray crystal structure of DHDPR from other organisms. This increased knowledge of the structure and function of plant lysine biosynthetic enzymes will aid future work aimed at improving primary production.

	Characterisation of the first enzymes committed to lysine biosynthesis in Arabidopsis thaliana.,Griffin MD, Billakanti JM, Wason A, Keller S, Mertens HD, Atkinson SC, Dobson RC, Perugini MA, Gerrard JA, Pearce FG PLoS One. 2012;7(7):e40318. doi: 10.1371/journal.pone.0040318. Epub 2012 Jul 5. PMID:22792278<ref>PMID:22792278</ref>

	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~
	~~</div>~~
	~~<div class="pdbe-citations 4dpp" style="background-color:#fffaf0;"></div>~~

	==See Also==		==See Also==
	*[[Dihydrodipicolinate synthase\|Dihydrodipicolinate synthase]]		*[[Dihydrodipicolinate synthase\|Dihydrodipicolinate synthase]]
	~~== References ==~~
	~~<references/>~~
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 08:33, 21 September 2022

2022-09-21T08:33:28Z

← Older revision		Revision as of 08:33, 21 September 2022
Line 1:		Line 1:

	==The structure of dihydrodipicolinate synthase 2 from Arabidopsis thaliana==		==The structure of dihydrodipicolinate synthase 2 from Arabidopsis thaliana==
	<StructureSection load='4dpp' size='340' side='right' caption='[[4dpp]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='4dpp' size='340' side='right'caption='[[4dpp]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4dpp]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Arath Arath~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DPP OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4DPP FirstGlance]. <br>		<table><tr><td colspan='2'>[[4dpp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DPP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DPP FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene~~></td></tr>~~		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4dpq\|4dpq]]</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=4dpp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dpp OCA], [https://pdbe.org/4dpp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dpp RCSB], [https://www.ebi.ac.uk/pdbsum/4dpp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dpp ProSAT]</span></td></tr>
	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">DHDPS2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</td></tr>~~
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/4-hydroxy-tetrahydrodipicolinate_synthase 4-hydroxy-tetrahydrodipicolinate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.3.3.7 4.3.3.7] </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=4dpp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dpp OCA], [~~http~~://pdbe.org/4dpp PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4dpp RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4dpp PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4dpp ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[~~http~~://www.uniprot.org/uniprot/DAPA2_ARATH DAPA2_ARATH]] Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA) (By similarity).		[[https://www.uniprot.org/uniprot/DAPA2_ARATH DAPA2_ARATH]] Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA) (By similarity).
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 28:		Line 25:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~4-hydroxy-tetrahydrodipicolinate synthase~~]]		[[Category: Arabidopsis thaliana]]
	[[Category: ~~Arath~~]]		[[Category: Large Structures]]
	[[Category: Billakanti~~, J M~~]]		[[Category: Billakanti JM]]
	[[Category: Dobson~~, R C.J~~]]		[[Category: Dobson RCJ]]
	[[Category: Gerrard~~, J A~~]]		[[Category: Gerrard JA]]
	[[Category: Griffin~~, M D.W~~]]		[[Category: Griffin MDW]]
	[[Category: Pearce~~, F G]]~~		[[Category: Pearce FG]]
	~~[[Category: Amino-acid biosynthesis]]~~
	~~[[Category: Chloroplast]]~~
	~~[[Category: Class i aldolase]]~~
	~~[[Category: Lyase~~]]

OCA at 12:09, 4 August 2016

2016-08-04T12:09:12Z

← Older revision		Revision as of 12:09, 4 August 2016
Line 1:		Line 1:

	==The structure of dihydrodipicolinate synthase 2 from Arabidopsis thaliana==		==The structure of dihydrodipicolinate synthase 2 from Arabidopsis thaliana==
	<StructureSection load='4dpp' size='340' side='right' caption='[[4dpp]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='4dpp' size='340' side='right' caption='[[4dpp]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4dpp]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Arabidopsis_thaliana Arabidopsis thaliana~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DPP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4DPP FirstGlance]. <br>		<table><tr><td colspan='2'>[[4dpp]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DPP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4DPP FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4dpq\|4dpq]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4dpq\|4dpq]]</td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">DHDPS2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ~~Arabidopsis thaliana~~])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">DHDPS2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/4-hydroxy-tetrahydrodipicolinate_synthase 4-hydroxy-tetrahydrodipicolinate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.3.3.7 4.3.3.7] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/4-hydroxy-tetrahydrodipicolinate_synthase 4-hydroxy-tetrahydrodipicolinate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.3.3.7 4.3.3.7] </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=4dpp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dpp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4dpp RCSB], [http://www.ebi.ac.uk/pdbsum/4dpp 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=4dpp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dpp OCA], [http://pdbe.org/4dpp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4dpp RCSB], [http://www.ebi.ac.uk/pdbsum/4dpp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4dpp 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 4dpp" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 27:		Line 29:
	</StructureSection>		</StructureSection>
	[[Category: 4-hydroxy-tetrahydrodipicolinate synthase]]		[[Category: 4-hydroxy-tetrahydrodipicolinate synthase]]
	[[Category: ~~Arabidopsis thaliana~~]]		[[Category: Arath]]
	[[Category: Billakanti, J M]]		[[Category: Billakanti, J M]]
	[[Category: Dobson, R C.J]]		[[Category: Dobson, R C.J]]

OCA at 09:10, 25 December 2014

2014-12-25T09:10:58Z

← Older revision		Revision as of 09:10, 25 December 2014
Line 1:		Line 1:
	~~{{STRUCTURE_4dpp\| PDB~~=4dpp \| ~~SCENE~~= }}		==The structure of dihydrodipicolinate synthase 2 from Arabidopsis thaliana==
	===~~The~~ structure ~~of dihydrodipicolinate synthase 2~~ from Arabidopsis thaliana===		<StructureSection load='4dpp' size='340' side='right' caption='[[4dpp]], [[Resolution\|resolution]] 2.00Å' scene=''>
	~~{{ABSTRACT_PUBMED_22792278}}~~		== Structural highlights ==
			<table><tr><td colspan='2'>[[4dpp]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DPP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4DPP FirstGlance]. <br>
			</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
			<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4dpq\|4dpq]]</td></tr>
			<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">DHDPS2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 Arabidopsis thaliana])</td></tr>
			<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/4-hydroxy-tetrahydrodipicolinate_synthase 4-hydroxy-tetrahydrodipicolinate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.3.3.7 4.3.3.7] </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=4dpp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dpp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4dpp RCSB], [http://www.ebi.ac.uk/pdbsum/4dpp PDBsum]</span></td></tr>
			</table>
			== Function ==
			[[http://www.uniprot.org/uniprot/DAPA2_ARATH DAPA2_ARATH]] Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA) (By similarity).
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			In plants, the lysine biosynthetic pathway is an attractive target for both the development of herbicides and increasing the nutritional value of crops given that lysine is a limiting amino acid in cereals. Dihydrodipicolinate synthase (DHDPS) and dihydrodipicolinate reductase (DHDPR) catalyse the first two committed steps of lysine biosynthesis. Here, we carry out for the first time a comprehensive characterisation of the structure and activity of both DHDPS and DHDPR from Arabidopsis thaliana. The A. thaliana DHDPS enzyme (At-DHDPS2) has similar activity to the bacterial form of the enzyme, but is more strongly allosterically inhibited by (S)-lysine. Structural studies of At-DHDPS2 show (S)-lysine bound at a cleft between two monomers, highlighting the allosteric site; however, unlike previous studies, binding is not accompanied by conformational changes, suggesting that binding may cause changes in protein dynamics rather than large conformation changes. DHDPR from A. thaliana (At-DHDPR2) has similar specificity for both NADH and NADPH during catalysis, and has tighter binding of substrate than has previously been reported. While all known bacterial DHDPR enzymes have a tetrameric structure, analytical ultracentrifugation, and scattering data unequivocally show that At-DHDPR2 exists as a dimer in solution. The exact arrangement of the dimeric protein is as yet unknown, but ab initio modelling of x-ray scattering data is consistent with an elongated structure in solution, which does not correspond to any of the possible dimeric pairings observed in the X-ray crystal structure of DHDPR from other organisms. This increased knowledge of the structure and function of plant lysine biosynthetic enzymes will aid future work aimed at improving primary production.

	~~==Function==~~		Characterisation of the first enzymes committed to lysine biosynthesis in Arabidopsis thaliana.,Griffin MD, Billakanti JM, Wason A, Keller S, Mertens HD, Atkinson SC, Dobson RC, Perugini MA, Gerrard JA, Pearce FG PLoS One. 2012;7(7):e40318. doi: 10.1371/journal.pone.0040318. Epub 2012 Jul 5. PMID:22792278<ref>PMID:22792278</ref>
	~~[[http~~:/~~/www~~.~~uniprot~~.~~org~~/~~uniprot/DAPA2_ARATH DAPA2_ARATH]] Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA) (By similarity).~~

	~~==About this Structure==~~		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	~~[[4dpp]] is~~ a ~~2 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]~~. ~~Full crystallographic information is available from [http:/~~/~~oca.weizmann.ac.il/oca-bin/ocashort?id=4DPP OCA].~~		</div>

	==See Also==		==See Also==
	*[[Dihydrodipicolinate ~~Synthase~~\|Dihydrodipicolinate ~~Synthase~~]]		*[[Dihydrodipicolinate synthase\|Dihydrodipicolinate synthase]]
			== References ==
	==~~Reference~~==		<references/>
	~~<ref group="xtra">PMID:022792278</ref>~~<references ~~group="xtra"~~/><~~references~~/>		__TOC__
			</StructureSection>
	[[Category: 4-hydroxy-tetrahydrodipicolinate synthase]]		[[Category: 4-hydroxy-tetrahydrodipicolinate synthase]]
	[[Category: Arabidopsis thaliana]]		[[Category: Arabidopsis thaliana]]
	[[Category: Billakanti, J M.]]		[[Category: Billakanti, J M]]
	[[Category: Dobson, R C.J.]]		[[Category: Dobson, R C.J]]
	[[Category: Gerrard, J A.]]		[[Category: Gerrard, J A]]
	[[Category: Griffin, M D.W.]]		[[Category: Griffin, M D.W]]
	[[Category: Pearce, F G.]]		[[Category: Pearce, F G]]
	[[Category: Amino-acid biosynthesis]]		[[Category: Amino-acid biosynthesis]]
	[[Category: Chloroplast]]		[[Category: Chloroplast]]
	[[Category: Class i aldolase]]		[[Category: Class i aldolase]]
	[[Category: Lyase]]		[[Category: Lyase]]

OCA at 08:45, 4 September 2013

2013-09-04T08:45:03Z

← Older revision		Revision as of 08:45, 4 September 2013
Line 1:		Line 1:
	~~[[Image:4dpp.png\|left\|200px]]~~

	{{STRUCTURE_4dpp\| PDB=4dpp \| SCENE= }}		{{STRUCTURE_4dpp\| PDB=4dpp \| SCENE= }}

	===The structure of dihydrodipicolinate synthase 2 from Arabidopsis thaliana===		===The structure of dihydrodipicolinate synthase 2 from Arabidopsis thaliana===
			{{ABSTRACT_PUBMED_22792278}}

			==Function==
			[[http://www.uniprot.org/uniprot/DAPA2_ARATH DAPA2_ARATH]] Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA) (By similarity).

	==About this Structure==		==About this Structure==
Line 11:		Line 11:
	==See Also==		==See Also==
	*[[Dihydrodipicolinate Synthase\|Dihydrodipicolinate Synthase]]		*[[Dihydrodipicolinate Synthase\|Dihydrodipicolinate Synthase]]

			==Reference==
			<ref group="xtra">PMID:022792278</ref><references group="xtra"/><references/>
			[[Category: 4-hydroxy-tetrahydrodipicolinate synthase]]
	[[Category: Arabidopsis thaliana]]		[[Category: Arabidopsis thaliana]]
	~~[[Category: Dihydrodipicolinate synthase]]~~
	[[Category: Billakanti, J M.]]		[[Category: Billakanti, J M.]]
	[[Category: Dobson, R C.J.]]		[[Category: Dobson, R C.J.]]

OCA at 14:57, 20 October 2012

2012-10-20T14:57:43Z

← Older revision		Revision as of 14:57, 20 October 2012
Line 1:		Line 1:
	[[Image:4dpp.~~jpg~~\|left\|200px]]		[[Image:4dpp.png\|left\|200px]]

	{{STRUCTURE_4dpp\| PDB=4dpp \| SCENE= }}		{{STRUCTURE_4dpp\| PDB=4dpp \| SCENE= }}
Line 8:		Line 8:
	==About this Structure==		==About this Structure==
	[[4dpp]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DPP OCA].		[[4dpp]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DPP OCA].

			==See Also==
			*[[Dihydrodipicolinate Synthase\|Dihydrodipicolinate Synthase]]
	[[Category: Arabidopsis thaliana]]		[[Category: Arabidopsis thaliana]]
	[[Category: Dihydrodipicolinate synthase]]		[[Category: Dihydrodipicolinate synthase]]

OCA at 05:30, 18 July 2012

2012-07-18T05:30:14Z

← Older revision		Revision as of 05:30, 18 July 2012
Line 1:		Line 1:
	~~'''Unreleased structure'''~~		[[Image:4dpp.jpg\|left\|200px]]

	~~The entry~~ 4dpp ~~is ON HOLD~~ ~~until Paper Publication~~		{{STRUCTURE_4dpp\| PDB=4dpp \| SCENE= }}

	~~Authors: Griffin, M.D.W., Billakanti, J.M., Gerrard, J.A., Dobson, R.C.J., Pearce, F.G.~~		===The structure of dihydrodipicolinate synthase 2 from Arabidopsis thaliana===

	~~Description~~: ~~The structure of dihydrodipicolinate synthase 2~~ from Arabidopsis thaliana
			==About this Structure==
			[[4dpp]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DPP OCA].
			[[Category: Arabidopsis thaliana]]
			[[Category: Dihydrodipicolinate synthase]]
			[[Category: Billakanti, J M.]]
			[[Category: Dobson, R C.J.]]
			[[Category: Gerrard, J A.]]
			[[Category: Griffin, M D.W.]]
			[[Category: Pearce, F G.]]
			[[Category: Amino-acid biosynthesis]]
			[[Category: Chloroplast]]
			[[Category: Class i aldolase]]
			[[Category: Lyase]]

OCA at 08:24, 29 February 2012

2012-02-29T08:24:07Z

← Older revision		Revision as of 08:24, 29 February 2012
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

	The entry 4dpp is ON HOLD		The entry 4dpp is ON HOLD until Paper Publication

	Authors: Griffin, M.D.W., Billakanti, J.M., Gerrard, J.A., Dobson, R.C.J., Pearce, F.G.		Authors: Griffin, M.D.W., Billakanti, J.M., Gerrard, J.A., Dobson, R.C.J., Pearce, F.G.

	Description: The structure of dihydrodipicolinate synthase 2 from Arabidopsis thaliana		Description: The structure of dihydrodipicolinate synthase 2 from Arabidopsis thaliana

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

2012-02-22T07:32:20Z

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

← Older revision	Revision as of 07:32, 22 February 2012
(No difference)

OCA: New page: '''Unreleased structure''' The entry 4dpp is ON HOLD Authors: Griffin, M.D.W., Billakanti, J.M., Gerrard, J.A., Dobson, R.C.J., Pearce, F.G. Description: The structure of dihydrodipico...

2012-02-22T07:32:19Z

New page: '''Unreleased structure''' The entry 4dpp is ON HOLD Authors: Griffin, M.D.W., Billakanti, J.M., Gerrard, J.A., Dobson, R.C.J., Pearce, F.G. Description: The structure of dihydrodipico...

New page

'''Unreleased structure'''

The entry 4dpp is ON HOLD

Authors: Griffin, M.D.W., Billakanti, J.M., Gerrard, J.A., Dobson, R.C.J., Pearce, F.G.

Description: The structure of dihydrodipicolinate synthase 2 from Arabidopsis thaliana