1dhp - Revision history

OCA at 06:53, 7 February 2024

2024-02-07T06:53:53Z

←Older revision		Revision as of 06:53, 7 February 2024
Line 3:		Line 3:
	<StructureSection load='1dhp' size='340' side='right'caption='[[1dhp]], [[Resolution\|resolution]] 2.30Å' scene=''>		<StructureSection load='1dhp' size='340' side='right'caption='[[1dhp]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1dhp]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DHP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DHP FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1dhp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DHP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DHP FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=K:POTASSIUM+ION'>K</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]] 2.3Å</td></tr>
-	<tr id='~~activity~~'><td class="sblockLbl"><b>~~Activity~~:</b></td><td class="sblockDat"><~~span class~~='~~plainlinks~~'>[https://en.wikipedia.org/wiki/4-hydroxy-tetrahydrodipicolinate_synthase 4-hydroxy-tetrahydrodipicolinate synthase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.3.3.7 4.3.3.7] </~~span~~></td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</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=1dhp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dhp OCA], [https://pdbe.org/1dhp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dhp RCSB], [https://www.ebi.ac.uk/pdbsum/1dhp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dhp 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=1dhp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dhp OCA], [https://pdbe.org/1dhp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dhp RCSB], [https://www.ebi.ac.uk/pdbsum/1dhp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dhp ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/DAPA_ECOLI DAPA_ECOLI]] Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).<ref>PMID:20503968</ref> <ref>PMID:8993314</ref>	+	[https://www.uniprot.org/uniprot/DAPA_ECOLI DAPA_ECOLI] Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).<ref>PMID:20503968</ref> <ref>PMID:8993314</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 20:		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=1dhp 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=1dhp ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	The crystal structure of dihydrodipicolinate synthase from E. coli was determined by multiple isomorphous replacement methods. The structure was refined at a resolution of 2.5 A and the final R-factor is 19.6% for 32,190 reflections between 10.0 A and 2.5 A and F > 2 sigma (F). The crystallographic asymmetric unit contains two monomers related by approximate 2-fold symmetry. A tetramer with approximate 222 symmetry is built up by crystallographic symmetry. The tetramer is almost planar with no contacts between the subunits related by the non-crystallographic dyad. The active sites are accessible from a wide water-filled channel in the center of the tetramer. The dihydrodipicolinate synthase monomer is composed of two domains. Each polypeptide chain is folded into an 8-fold alpha/beta barrel and a C-terminal alpha-helical domain comprising residues 224 to 292. The fold is similar to that of N-acetylneuraminate lyase. The active site lysine 161 is located in the alpha/beta barrel and has access via two entrances from the C-terminal side of the barrel.
-
-	The crystal structure of dihydrodipicolinate synthase from Escherichia coli at 2.5 A resolution.,Mirwaldt C, Korndorfer I, Huber R J Mol Biol. 1995 Feb 10;246(1):227-39. PMID:7853400<ref>PMID:7853400</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1dhp" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 36:		Line 27:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~4-hydroxy-tetrahydrodipicolinate synthase~~]]	+	[[Category: Escherichia coli]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Huber, R]]	+	[[Category: Huber R]]
-	[[Category: Korndoerfer, I]]	+	[[Category: Korndoerfer I]]
-	[[Category: Mirwaldt, C]]	+	[[Category: Mirwaldt C]]
-	~~[[Category: Dihydrodipicolinate]]~~	+
-	~~[[Category: Synthase~~]]	+

OCA at 18:27, 10 March 2021

2021-03-10T18:27:30Z

←Older revision		Revision as of 18:27, 10 March 2021
Line 3:		Line 3:
	<StructureSection load='1dhp' size='340' side='right'caption='[[1dhp]], [[Resolution\|resolution]] 2.30Å' scene=''>		<StructureSection load='1dhp' size='340' side='right'caption='[[1dhp]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1dhp]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DHP OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1DHP FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1dhp]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DHP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DHP FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene></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'>[https://en.wikipedia.org/wiki/4-hydroxy-tetrahydrodipicolinate_synthase 4-hydroxy-tetrahydrodipicolinate synthase], with EC number [https://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=1dhp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dhp OCA], [~~http~~://pdbe.org/1dhp PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1dhp RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1dhp PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1dhp 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=1dhp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dhp OCA], [https://pdbe.org/1dhp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dhp RCSB], [https://www.ebi.ac.uk/pdbsum/1dhp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dhp ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/DAPA_ECOLI DAPA_ECOLI]] Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).<ref>PMID:20503968</ref> <ref>PMID:8993314</ref>	+	[[https://www.uniprot.org/uniprot/DAPA_ECOLI DAPA_ECOLI]] Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).<ref>PMID:20503968</ref> <ref>PMID:8993314</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 23:28, 5 June 2019

2019-06-05T23:28:58Z

←Older revision		Revision as of 23:28, 5 June 2019
Line 1:		Line 1:

	==DIHYDRODIPICOLINATE SYNTHASE==		==DIHYDRODIPICOLINATE SYNTHASE==
-	<StructureSection load='1dhp' size='340' side='right' caption='[[1dhp]], [[Resolution\|resolution]] 2.30Å' scene=''>	+	<StructureSection load='1dhp' size='340' side='right'caption='[[1dhp]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1dhp]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DHP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DHP FirstGlance]. <br>		<table><tr><td colspan='2'>[[1dhp]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DHP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DHP FirstGlance]. <br>
Line 14:		Line 14:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dh/1dhp_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dh/1dhp_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>
Line 37:		Line 37:
	</StructureSection>		</StructureSection>
	[[Category: 4-hydroxy-tetrahydrodipicolinate synthase]]		[[Category: 4-hydroxy-tetrahydrodipicolinate synthase]]
		+	[[Category: Large Structures]]
	[[Category: Huber, R]]		[[Category: Huber, R]]
	[[Category: Korndoerfer, I]]		[[Category: Korndoerfer, I]]

OCA at 04:04, 30 August 2017

2017-08-30T04:04:14Z

←Older revision		Revision as of 04:04, 30 August 2017
Line 1:		Line 1:
		+
	==DIHYDRODIPICOLINATE SYNTHASE==		==DIHYDRODIPICOLINATE SYNTHASE==
	<StructureSection load='1dhp' size='340' side='right' caption='[[1dhp]], [[Resolution\|resolution]] 2.30Å' scene=''>		<StructureSection load='1dhp' size='340' side='right' caption='[[1dhp]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1dhp]] is a 2 chain structure ~~with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]~~. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DHP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DHP FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1dhp]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DHP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DHP FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">DAPA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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=1dhp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dhp OCA], [http://pdbe.org/1dhp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1dhp RCSB], [http://www.ebi.ac.uk/pdbsum/1dhp 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=1dhp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dhp OCA], [http://pdbe.org/1dhp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1dhp RCSB], [http://www.ebi.ac.uk/pdbsum/1dhp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1dhp ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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=1dhp ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 36:		Line 36:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Bacillus coli migula 1895]]
	[[Category: 4-hydroxy-tetrahydrodipicolinate synthase]]		[[Category: 4-hydroxy-tetrahydrodipicolinate synthase]]
	[[Category: Huber, R]]		[[Category: Huber, R]]

OCA at 14:18, 11 September 2015

2015-09-11T14:18:41Z

←Older revision		Revision as of 14:18, 11 September 2015
Line 2:		Line 2:
	<StructureSection load='1dhp' size='340' side='right' caption='[[1dhp]], [[Resolution\|resolution]] 2.30Å' scene=''>		<StructureSection load='1dhp' size='340' side='right' caption='[[1dhp]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1dhp]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Escherichia_coli Escherichia~~ coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DHP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DHP FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1dhp]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DHP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DHP FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">DAPA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 ~~Escherichia~~ coli])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">DAPA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/~~Dihydrodipicolinate_synthase Dihydrodipicolinate~~ synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.52 4.2.1.52] </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=1dhp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dhp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1dhp RCSB], [http://www.ebi.ac.uk/pdbsum/1dhp 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=1dhp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dhp OCA], [http://pdbe.org/1dhp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1dhp RCSB], [http://www.ebi.ac.uk/pdbsum/1dhp 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 1dhp" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 35:		Line 36:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Dihydrodipicolinate synthase~~]]	+	[[Category: Bacillus coli migula 1895]]
-	[[Category: ~~Escherichia coli~~]]	+	[[Category: 4-hydroxy-tetrahydrodipicolinate synthase]]
	[[Category: Huber, R]]		[[Category: Huber, R]]
	[[Category: Korndoerfer, I]]		[[Category: Korndoerfer, I]]

OCA at 17:36, 25 December 2014

2014-12-25T17:36:32Z

←Older revision		Revision as of 17:36, 25 December 2014
Line 8:		Line 8:
	<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=1dhp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dhp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1dhp RCSB], [http://www.ebi.ac.uk/pdbsum/1dhp 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=1dhp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dhp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1dhp RCSB], [http://www.ebi.ac.uk/pdbsum/1dhp PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/DAPA_ECOLI DAPA_ECOLI]] Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).<ref>PMID:20503968</ref> <ref>PMID:8993314</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 22:36, 22 December 2014

2014-12-22T22:36:58Z

←Older revision		Revision as of 22:36, 22 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1dhp]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DHP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DHP FirstGlance]. <br>		<table><tr><td colspan='2'>[[1dhp]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DHP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DHP FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">DAPA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">DAPA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dihydrodipicolinate_synthase Dihydrodipicolinate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.52 4.2.1.52] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dihydrodipicolinate_synthase Dihydrodipicolinate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.52 4.2.1.52] </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=1dhp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dhp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1dhp RCSB], [http://www.ebi.ac.uk/pdbsum/1dhp 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=1dhp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dhp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1dhp RCSB], [http://www.ebi.ac.uk/pdbsum/1dhp PDBsum]</span></td></tr>
-	<table>	+	</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 35:		Line 35:
	[[Category: Dihydrodipicolinate synthase]]		[[Category: Dihydrodipicolinate synthase]]
	[[Category: Escherichia coli]]		[[Category: Escherichia coli]]
-	[[Category: Huber, R.]]	+	[[Category: Huber, R]]
-	[[Category: Korndoerfer, I.]]	+	[[Category: Korndoerfer, I]]
-	[[Category: Mirwaldt, C.]]	+	[[Category: Mirwaldt, C]]
	[[Category: Dihydrodipicolinate]]		[[Category: Dihydrodipicolinate]]
	[[Category: Synthase]]		[[Category: Synthase]]

OCA at 10:38, 3 October 2014

2014-10-03T10:38:18Z

←Older revision		Revision as of 10:38, 3 October 2014
Line 1:		Line 1:
-	[[~~Image:~~1dhp.~~png~~\|~~left~~\|200px]]	+	==DIHYDRODIPICOLINATE SYNTHASE==
		+	<StructureSection load='1dhp' size='340' side='right' caption='[[1dhp]], [[Resolution\|resolution]] 2.30Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1dhp]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DHP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DHP FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">DAPA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dihydrodipicolinate_synthase Dihydrodipicolinate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.52 4.2.1.52] </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=1dhp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dhp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1dhp RCSB], [http://www.ebi.ac.uk/pdbsum/1dhp 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/dh/1dhp_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 crystal structure of dihydrodipicolinate synthase from E. coli was determined by multiple isomorphous replacement methods. The structure was refined at a resolution of 2.5 A and the final R-factor is 19.6% for 32,190 reflections between 10.0 A and 2.5 A and F > 2 sigma (F). The crystallographic asymmetric unit contains two monomers related by approximate 2-fold symmetry. A tetramer with approximate 222 symmetry is built up by crystallographic symmetry. The tetramer is almost planar with no contacts between the subunits related by the non-crystallographic dyad. The active sites are accessible from a wide water-filled channel in the center of the tetramer. The dihydrodipicolinate synthase monomer is composed of two domains. Each polypeptide chain is folded into an 8-fold alpha/beta barrel and a C-terminal alpha-helical domain comprising residues 224 to 292. The fold is similar to that of N-acetylneuraminate lyase. The active site lysine 161 is located in the alpha/beta barrel and has access via two entrances from the C-terminal side of the barrel.

-	~~{{STRUCTURE_1dhp\| PDB=1dhp \| SCENE= }}~~	+	The crystal structure of dihydrodipicolinate synthase from Escherichia coli at 2.5 A resolution.,Mirwaldt C, Korndorfer I, Huber R J Mol Biol. 1995 Feb 10;246(1):227-39. PMID:7853400<ref>PMID:7853400</ref>

-	~~===DIHYDRODIPICOLINATE SYNTHASE===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_7853400}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[1dhp]] is~~ a ~~2 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Escherichia_coli Escherichia coli]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=1DHP OCA].~~	+

	==See Also==		==See Also==
-	*[[Dihydrodipicolinate ~~Synthase~~\|Dihydrodipicolinate ~~Synthase~~]]	+	*[[Dihydrodipicolinate synthase\|Dihydrodipicolinate synthase]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:007853400<~~/~~ref~~><~~references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Dihydrodipicolinate synthase]]		[[Category: Dihydrodipicolinate synthase]]
	[[Category: Escherichia coli]]		[[Category: Escherichia coli]]

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

2012-10-20T19:32:06Z

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

←Older revision

Revision as of 19:32, 20 October 2012

OCA at 19:32, 20 October 2012

2012-10-20T19:32:03Z

←Older revision		Revision as of 19:32, 20 October 2012
Line 1:		Line 1:
-	{{Seed}}
	[[Image:1dhp.png\|left\|200px]]		[[Image:1dhp.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_1dhp", 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_1dhp\| PDB=1dhp \| SCENE= }}		{{STRUCTURE_1dhp\| PDB=1dhp \| SCENE= }}

	===DIHYDRODIPICOLINATE SYNTHASE===		===DIHYDRODIPICOLINATE SYNTHASE===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_7853400}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 7853400 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_7853400}}		{{ABSTRACT_PUBMED_7853400}}

	==About this Structure==		==About this Structure==
-	~~1DHP~~ is a 2 ~~chains~~ structure ~~of sequences~~ from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DHP OCA].	+	[[1dhp]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DHP OCA].
		+
		+	==See Also==
		+	*[[Dihydrodipicolinate Synthase\|Dihydrodipicolinate Synthase]]

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~7853400~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:007853400</ref><references group="xtra"/>
	[[Category: Dihydrodipicolinate synthase]]		[[Category: Dihydrodipicolinate synthase]]
	[[Category: Escherichia coli]]		[[Category: Escherichia coli]]
Line 31:		Line 22:
	[[Category: Dihydrodipicolinate]]		[[Category: Dihydrodipicolinate]]
	[[Category: Synthase]]		[[Category: Synthase]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 00:24:01 2009''