2x65 - Revision history

OCA at 10:24, 20 December 2023

2023-12-20T10:24:32Z

←Older revision		Revision as of 10:24, 20 December 2023
Line 3:		Line 3:
	<StructureSection load='2x65' size='340' side='right'caption='[[2x65]], [[Resolution\|resolution]] 2.10Å' scene=''>		<StructureSection load='2x65' size='340' side='right'caption='[[2x65]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2x65]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Thema Thema~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X65 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2X65 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2x65]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima_MSB8 Thermotoga maritima MSB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X65 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2X65 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=M1P:ALPHA-D-MANNOSE+1-PHOSPHATE'>M1P</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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;'>[[2x5z\|2x5z]], [[2x5s\|2x5s]], [[2x60\|2x60]]</div></td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=M1P:ALPHA-D-MANNOSE+1-PHOSPHATE'>M1P</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Mannose-1-phosphate_guanylyltransferase Mannose-1-phosphate guanylyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.13 2.7.7.13] </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=2x65 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x65 OCA], [https://pdbe.org/2x65 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2x65 RCSB], [https://www.ebi.ac.uk/pdbsum/2x65 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2x65 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=2x65 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x65 OCA], [https://pdbe.org/2x65 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2x65 RCSB], [https://www.ebi.ac.uk/pdbsum/2x65 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2x65 ProSAT]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/Q9X0C3_THEMA Q9X0C3_THEMA]
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 33:		Line 34:
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Mannose-1-phosphate guanylyltransferase]]~~	+	[[Category: Thermotoga maritima MSB8]]
-	~~[[Category: Thema~~]]	+	[[Category: Bourne Y]]
-	[[Category: Bourne, Y]]	+	[[Category: Kuhn P]]
-	[[Category: Kuhn, P]]	+	[[Category: Lesley S]]
-	[[Category: Lesley, S]]	+	[[Category: Pelissier MC]]
-	[[Category: Pelissier~~, M C]]~~	+
-	~~[[Category: Nucleotidyltransferase]]~~	+
-	~~[[Category: Transferase~~]]	+

OCA at 10:46, 13 April 2022

2022-04-13T10:46:17Z

←Older revision		Revision as of 10:46, 13 April 2022
Line 3:		Line 3:
	<StructureSection load='2x65' size='340' side='right'caption='[[2x65]], [[Resolution\|resolution]] 2.10Å' scene=''>		<StructureSection load='2x65' size='340' side='right'caption='[[2x65]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2x65]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Thema Thema]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X65 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=2X65 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2x65]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thema Thema]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X65 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2X65 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=M1P:ALPHA-D-MANNOSE+1-PHOSPHATE'>M1P</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=M1P:ALPHA-D-MANNOSE+1-PHOSPHATE'>M1P</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2x5z\|2x5z]], [[2x5s\|2x5s]], [[2x60\|2x60]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2x5z\|2x5z]], [[2x5s\|2x5s]], [[2x60\|2x60]]</div></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Mannose-1-phosphate_guanylyltransferase Mannose-1-phosphate guanylyltransferase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.13 2.7.7.13] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Mannose-1-phosphate_guanylyltransferase Mannose-1-phosphate guanylyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.13 2.7.7.13] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=2x65 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x65 OCA], [~~http~~://pdbe.org/2x65 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2x65 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2x65 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2x65 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=2x65 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x65 OCA], [https://pdbe.org/2x65 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2x65 RCSB], [https://www.ebi.ac.uk/pdbsum/2x65 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2x65 ProSAT]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==

OCA at 15:05, 8 July 2020

2020-07-08T15:05:40Z

←Older revision		Revision as of 15:05, 8 July 2020
Line 1:		Line 1:

	==Crystal structure of T. maritima GDP-mannose pyrophosphorylase in complex with mannose-1-phosphate.==		==Crystal structure of T. maritima GDP-mannose pyrophosphorylase in complex with mannose-1-phosphate.==
-	<StructureSection load='2x65' size='340' side='right' caption='[[2x65]], [[Resolution\|resolution]] 2.10Å' scene=''>	+	<StructureSection load='2x65' size='340' side='right'caption='[[2x65]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2x65]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Thema Thema]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X65 OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2X65 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2x65]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Thema Thema]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X65 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2X65 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=M1P:ALPHA-D-MANNOSE+1-PHOSPHATE'>M1P</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=M1P:ALPHA-D-MANNOSE+1-PHOSPHATE'>M1P</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2x5z\|2x5z]], [[2x5s\|2x5s]], [[2x60\|2x60]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2x5z\|2x5z]], [[2x5s\|2x5s]], [[2x60\|2x60]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Mannose-1-phosphate_guanylyltransferase Mannose-1-phosphate guanylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.13 2.7.7.13] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Mannose-1-phosphate_guanylyltransferase Mannose-1-phosphate guanylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.13 2.7.7.13] </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=2x65 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x65 OCA], [http://pdbe.org/2x65 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2x65 RCSB], [http://www.ebi.ac.uk/pdbsum/2x65 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2x65 ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2x65 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x65 OCA], [http://pdbe.org/2x65 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2x65 RCSB], [http://www.ebi.ac.uk/pdbsum/2x65 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2x65 ProSAT]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
Line 32:		Line 32:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Mannose-1-phosphate guanylyltransferase]]		[[Category: Mannose-1-phosphate guanylyltransferase]]
	[[Category: Thema]]		[[Category: Thema]]

OCA at 09:34, 3 October 2018

2018-10-03T09:34:59Z

←Older revision		Revision as of 09:34, 3 October 2018
Line 1:		Line 1:

-	==~~CRYSTAL STRUCTURE OF~~ T. ~~MARITIMA~~ GDP-~~MANNOSE PYROPHOSPHORYLASE IN COMPLEX WITH MANNOSE~~-1-~~PHOSPHATE~~.==	+	==Crystal structure of T. maritima GDP-mannose pyrophosphorylase in complex with mannose-1-phosphate.==
	<StructureSection load='2x65' size='340' side='right' caption='[[2x65]], [[Resolution\|resolution]] 2.10Å' scene=''>		<StructureSection load='2x65' size='340' side='right' caption='[[2x65]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
Line 13:		Line 13:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/x6/2x65_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/x6/2x65_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>

OCA at 21:04, 11 August 2016

2016-08-11T21:04:24Z

←Older revision		Revision as of 21:04, 11 August 2016
Line 1:		Line 1:
		+
	==CRYSTAL STRUCTURE OF T. MARITIMA GDP-MANNOSE PYROPHOSPHORYLASE IN COMPLEX WITH MANNOSE-1-PHOSPHATE.==		==CRYSTAL STRUCTURE OF T. MARITIMA GDP-MANNOSE PYROPHOSPHORYLASE IN COMPLEX WITH MANNOSE-1-PHOSPHATE.==
	<StructureSection load='2x65' size='340' side='right' caption='[[2x65]], [[Resolution\|resolution]] 2.10Å' scene=''>		<StructureSection load='2x65' size='340' side='right' caption='[[2x65]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2x65]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Thermotoga_maritima Thermotoga maritima~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X65 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2X65 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2x65]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Thema Thema]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X65 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2X65 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=M1P:ALPHA-D-MANNOSE+1-PHOSPHATE'>M1P</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=M1P:ALPHA-D-MANNOSE+1-PHOSPHATE'>M1P</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2x5z\|2x5z]], [[2x5s\|2x5s]], [[2x60\|2x60]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2x5z\|2x5z]], [[2x5s\|2x5s]], [[2x60\|2x60]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Mannose-1-phosphate_guanylyltransferase Mannose-1-phosphate guanylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.13 2.7.7.13] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Mannose-1-phosphate_guanylyltransferase Mannose-1-phosphate guanylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.13 2.7.7.13] </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=2x65 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x65 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2x65 RCSB], [http://www.ebi.ac.uk/pdbsum/2x65 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=2x65 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x65 OCA], [http://pdbe.org/2x65 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2x65 RCSB], [http://www.ebi.ac.uk/pdbsum/2x65 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2x65 ProSAT]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
Line 16:		Line 17:
	<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=2x65 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 26:		Line 27:
	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 2x65" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
Line 31:		Line 33:
	</StructureSection>		</StructureSection>
	[[Category: Mannose-1-phosphate guanylyltransferase]]		[[Category: Mannose-1-phosphate guanylyltransferase]]
-	[[Category: ~~Thermotoga maritima~~]]	+	[[Category: Thema]]
	[[Category: Bourne, Y]]		[[Category: Bourne, Y]]
	[[Category: Kuhn, P]]		[[Category: Kuhn, P]]

OCA at 07:57, 25 January 2015

2015-01-25T07:57:05Z

←Older revision		Revision as of 07:57, 25 January 2015
Line 32:		Line 32:
	[[Category: Mannose-1-phosphate guanylyltransferase]]		[[Category: Mannose-1-phosphate guanylyltransferase]]
	[[Category: Thermotoga maritima]]		[[Category: Thermotoga maritima]]
-	[[Category: Bourne, Y.]]	+	[[Category: Bourne, Y]]
-	[[Category: Kuhn, P.]]	+	[[Category: Kuhn, P]]
-	[[Category: Lesley, S.]]	+	[[Category: Lesley, S]]
-	[[Category: Pelissier, M C.]]	+	[[Category: Pelissier, M C]]
	[[Category: Nucleotidyltransferase]]		[[Category: Nucleotidyltransferase]]
	[[Category: Transferase]]		[[Category: Transferase]]

OCA at 12:58, 22 October 2014

2014-10-22T12:58:34Z

←Older revision		Revision as of 12:58, 22 October 2014
Line 1:		Line 1:
-	[[~~Image:~~2x65.~~png~~\|~~left~~\|200px]]	+	==CRYSTAL STRUCTURE OF T. MARITIMA GDP-MANNOSE PYROPHOSPHORYLASE IN COMPLEX WITH MANNOSE-1-PHOSPHATE.==
		+	<StructureSection load='2x65' size='340' side='right' caption='[[2x65]], [[Resolution\|resolution]] 2.10Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[2x65]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X65 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2X65 FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=M1P:ALPHA-D-MANNOSE+1-PHOSPHATE'>M1P</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2x5z\|2x5z]], [[2x5s\|2x5s]], [[2x60\|2x60]]</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Mannose-1-phosphate_guanylyltransferase Mannose-1-phosphate guanylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.13 2.7.7.13] </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=2x65 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x65 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2x65 RCSB], [http://www.ebi.ac.uk/pdbsum/2x65 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/x6/2x65_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 ==
		+	GMP catalyzes the formation of GDP-Man, a fundamental precursor for protein glycosylation and bacterial cell wall and capsular polysaccharide biosynthesis. Crystal structures of GMP from the thermophilic bacterium Thermotoga maritima in the apo form, in complex with the substrates mannose-1-phosphate or GTP and bound with the end product GDP-Man in the presence of the essential divalent cation Mg(2+), were solved in the 2.1-2.8 A resolution range. The T. maritima GMP molecule is organized in two separate domains: a N-terminal Rossman fold-like domain and a C-terminal left-handed beta-helix domain. Two molecules associate into a dimer through a tail-to-tail arrangement of the C-terminal domains. Comparative analysis of the structures along with characterization of enzymatic parameters reveals the bases of substrate specificity of this class of sugar nucleotidyltransferases. In particular, substrate and product binding are associated with significant changes in the conformation of loop regions lining the active center and in the relative orientation of the two domains. Involvement of both the N- and C-terminal domains, coupled to the catalytic role of a bivalent metal ion, highlights the catalytic features of bacterial GMPs compared with other members of the pyrophosphorylase superfamily.

-	~~{{STRUCTURE_2x65\| PDB=2x65 \| SCENE= }}~~	+	Structural insights into the catalytic mechanism of bacterial guanosine-diphospho-D-mannose pyrophosphorylase and its regulation by divalent ions.,Pelissier MC, Lesley SA, Kuhn P, Bourne Y J Biol Chem. 2010 Aug 27;285(35):27468-76. Epub 2010 Jun 23. PMID:20573954<ref>PMID:20573954</ref>

-	~~===CRYSTAL STRUCTURE OF T. MARITIMA GDP-MANNOSE PYROPHOSPHORYLASE IN COMPLEX WITH MANNOSE-1-PHOSPHATE.===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_20573954}}~~	+	== References ==
-		+	<references/>
-	~~==About this Structure==~~	+	__TOC__
-	~~[[2x65]] is~~ a ~~2 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Thermotoga_maritima Thermotoga maritima]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=2X65 OCA].~~	+	</StructureSection>
-		+
-	==~~Reference~~==	+
-	<~~ref group="xtra">PMID:020573954<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Mannose-1-phosphate guanylyltransferase]]		[[Category: Mannose-1-phosphate guanylyltransferase]]
	[[Category: Thermotoga maritima]]		[[Category: Thermotoga maritima]]

OCA: Protected "2x65" [edit=sysop:move=sysop]

2013-01-07T23:04:29Z

Protected "2x65" [edit=sysop:move=sysop]

←Older revision

Revision as of 23:04, 7 January 2013

OCA at 23:04, 7 January 2013

2013-01-07T23:04:26Z

←Older revision		Revision as of 23:04, 7 January 2013
Line 1:		Line 1:
-	{{Seed}}
	[[Image:2x65.png\|left\|200px]]		[[Image:2x65.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_2x65", 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_2x65\| PDB=2x65 \| SCENE= }}		{{STRUCTURE_2x65\| PDB=2x65 \| SCENE= }}

	===CRYSTAL STRUCTURE OF T. MARITIMA GDP-MANNOSE PYROPHOSPHORYLASE IN COMPLEX WITH MANNOSE-1-PHOSPHATE.===		===CRYSTAL STRUCTURE OF T. MARITIMA GDP-MANNOSE PYROPHOSPHORYLASE IN COMPLEX WITH MANNOSE-1-PHOSPHATE.===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_20573954}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 20573954 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_20573954}}		{{ABSTRACT_PUBMED_20573954}}

	==About this Structure==		==About this Structure==
-	~~2X65~~ is a 2 ~~chains~~ structure with ~~sequences~~ from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X65 OCA].	+	[[2x65]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X65 OCA].

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~20573954~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:020573954</ref><references group="xtra"/>
	[[Category: Mannose-1-phosphate guanylyltransferase]]		[[Category: Mannose-1-phosphate guanylyltransferase]]
	[[Category: Thermotoga maritima]]		[[Category: Thermotoga maritima]]
Line 30:		Line 18:
	[[Category: Lesley, S.]]		[[Category: Lesley, S.]]
	[[Category: Pelissier, M C.]]		[[Category: Pelissier, M C.]]
-	[[Category: Gdp-mannose biosynthesis]]
	[[Category: Nucleotidyltransferase]]		[[Category: Nucleotidyltransferase]]
	[[Category: Transferase]]		[[Category: Transferase]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 7 08:15:23 2010''

OCA at 04:09, 7 July 2010

2010-07-07T04:09:53Z

←Older revision		Revision as of 04:09, 7 July 2010
Line 1:		Line 1:
	{{Seed}}		{{Seed}}
-	[[Image:2x65.~~jpg~~\|left\|200px]]	+	[[Image:2x65.png\|left\|200px]]

	<!--		<!--
Line 12:		Line 12:
	===CRYSTAL STRUCTURE OF T. MARITIMA GDP-MANNOSE PYROPHOSPHORYLASE IN COMPLEX WITH MANNOSE-1-PHOSPHATE.===		===CRYSTAL STRUCTURE OF T. MARITIMA GDP-MANNOSE PYROPHOSPHORYLASE IN COMPLEX WITH MANNOSE-1-PHOSPHATE.===

		+
		+	<!--
		+	The line below this paragraph, {{ABSTRACT_PUBMED_20573954}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 20573954 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_20573954}}

	==About this Structure==		==About this Structure==
	2X65 is a 2 chains structure with sequences from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X65 OCA].		2X65 is a 2 chains structure with sequences from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X65 OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:20573954</ref><references group="xtra"/>
	[[Category: Mannose-1-phosphate guanylyltransferase]]		[[Category: Mannose-1-phosphate guanylyltransferase]]
	[[Category: Thermotoga maritima]]		[[Category: Thermotoga maritima]]
Line 25:		Line 34:
	[[Category: Transferase]]		[[Category: Transferase]]

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed ~~Jun 23~~ 08:47:02 2010''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 7 08:15:23 2010''