3ea2 - Revision history

OCA at 09:46, 21 February 2024

2024-02-21T09:46:06Z

← Older revision		Revision as of 09:46, 21 February 2024
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	<StructureSection load='3ea2' size='340' side='right'caption='[[3ea2]], [[Resolution\|resolution]] 1.95Å' scene=''>		<StructureSection load='3ea2' size='340' side='right'caption='[[3ea2]], [[Resolution\|resolution]] 1.95Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3ea2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/~~"bacillus_cereus_var._thuringiensis"_smith_et_al._1952 "bacillus cereus var.~~ thuringiensis~~" smith et al. 1952~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EA2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EA2 FirstGlance]. <br>		<table><tr><td colspan='2'>[[3ea2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_thuringiensis Bacillus thuringiensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EA2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EA2 FirstGlance]. <br>
	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=INS:1,2,3,4,5,6~~-~~HEXAHYDROXY-CYCLOHEXANE'>INS</scene>~~, ~~<scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 1.95Å</td></tr>
	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"><~~div style~~='~~overflow~~: ~~auto; max~~-~~height: 3em;~~'>~~[[3ea1\|3ea1]], [[3ea3\|3ea3]]~~</~~div~~><~~/td></tr>~~		<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=INS:1,2,3,4,5,6-HEXAHYDROXY-CYCLOHEXANE'>INS</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
	~~<tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b></td><td class="sblockDat"><span class='plainlinks~~'>[https://en.wikipedia.org/wiki/Phosphatidylinositol_diacylglycerol-lyase Phosphatidylinositol diacylglycerol-lyase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.6.1.13 4.6.1.13] </~~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=3ea2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ea2 OCA], [https://pdbe.org/3ea2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ea2 RCSB], [https://www.ebi.ac.uk/pdbsum/3ea2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ea2 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=3ea2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ea2 OCA], [https://pdbe.org/3ea2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ea2 RCSB], [https://www.ebi.ac.uk/pdbsum/3ea2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ea2 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[https://www.uniprot.org/uniprot/PLC_BACTU PLC_BACTU]] Cleaves glycosylphosphatidylinositol (GPI) and phosphatidylinositol (PI) anchors but not PI phosphates.		[https://www.uniprot.org/uniprot/PLC_BACTU PLC_BACTU] Cleaves glycosylphosphatidylinositol (GPI) and phosphatidylinositol (PI) anchors but not PI phosphates.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	</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=3ea2 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=3ea2 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	~~<div style="background-color:#fffaf0;">~~
	~~== Publication Abstract from PubMed ==~~
	Cleavage of phosphatidylinositol (PI) to inositol 1,2-(cyclic)-phosphate (cIP) and cIP hydrolysis to inositol 1-phosphate by Bacillus thuringiensis phosphatidylinositol-specific phospholipase C are activated by the enzyme binding to phosphatidylcholine (PC) surfaces. Part of this reflects improved binding of the protein to interfaces. However, crystallographic analysis of an interfacially impaired phosphatidylinositol-specific phospholipase (W47A/W242A) suggested protein dimerization might occur on the membrane. In the W47A/W242A dimer, four tyrosine residues from one monomer interact with the same tyrosine cluster of the other, forming a tight dimer interface close to the membrane binding regions. We have constructed mutant proteins in which two or more of these tyrosine residues have been replaced with serine. Phospholipid binding and enzymatic activity of these mutants have been examined to assess the importance of these residues to enzyme function. Replacing two tyrosines had small effects on enzyme activity. However, removal of three or four tyrosine residues weakened PC binding and reduced PI cleavage by the enzyme as well as PC activation of cIP hydrolysis. Crystal structures of Y247S/Y251S in the absence and presence of myo-inositol as well as Y246S/Y247S/Y248S/Y251S indicate that both mutant proteins crystallized as monomers, were very similar to one another, and had no change in the active site region. Kinetic assays, lipid binding, and structural results indicate that either (i) a specific PC binding site, critical for vesicle activities and cIP activation, has been impaired, or (ii) the reduced dimerization potential for Y246S/Y247S/Y248S and Y246S/Y247S/Y248S/Y251S is responsible for their reduced catalytic activity in all assay systems.

	Modulation of Bacillus thuringiensis phosphatidylinositol-specific phospholipase C activity by mutations in the putative dimerization interface.,Shi X, Shao C, Zhang X, Zambonelli C, Redfield AG, Head JF, Seaton BA, Roberts MF J Biol Chem. 2009 Jun 5;284(23):15607-18. Epub 2009 Apr 15. PMID:19369255<ref>PMID:19369255</ref>

	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~
	~~</div>~~
	~~<div class="pdbe-citations 3ea2" style="background-color:#fffaf0;"></div>~~

	==See Also==		==See Also==
	*[[Phospholipase C\|Phospholipase C]]		*[[Phospholipase C\|Phospholipase C]]
	~~== References ==~~
	~~<references/>~~
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Bacillus ~~cereus var.~~ thuringiensis ~~smith et al. 1952~~]]		[[Category: Bacillus thuringiensis]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	~~[[Category: Phosphatidylinositol diacylglycerol-lyase]]~~		[[Category: Head JF]]
	[[Category: Head~~, J F~~]]		[[Category: Redfied AG]]
	[[Category: Redfied~~, A G~~]]		[[Category: Roberts MF]]
	[[Category: Roberts~~, M F~~]]		[[Category: Seaton BA]]
	[[Category: Seaton~~, B A~~]]		[[Category: Shao C]]
	[[Category: Shao, C]]		[[Category: Shi X]]
	[[Category: Shi, X]]		[[Category: Zambonelli C]]
	[[Category: Zambonelli, C]]		[[Category: Zhang X]]
	[[Category: Zhang, X]]
	~~[[Category: Dimer]]~~
	~~[[Category: Interfacially impaired]]~~
	~~[[Category: Lipid degradation]]~~
	~~[[Category: Lyase]]~~
	~~[[Category: Membrane binding]]~~
	~~[[Category: Myo-inositol]]~~
	~~[[Category: Phosphatidylinositol-specific phospholipase c]]~~
	~~[[Category: Pi-plc]]~~
	~~[[Category: Secreted]]~~
	~~[[Category: Tim barrel~~]]

OCA at 19:37, 20 October 2021

2021-10-20T19:37:31Z

← Older revision		Revision as of 19:37, 20 October 2021
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	<StructureSection load='3ea2' size='340' side='right'caption='[[3ea2]], [[Resolution\|resolution]] 1.95Å' scene=''>		<StructureSection load='3ea2' size='340' side='right'caption='[[3ea2]], [[Resolution\|resolution]] 1.95Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3ea2]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/"bacillus_cereus_var._thuringiensis"_smith_et_al._1952 "bacillus cereus var. thuringiensis" smith et al. 1952]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EA2 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3EA2 FirstGlance]. <br>		<table><tr><td colspan='2'>[[3ea2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_cereus_var._thuringiensis"_smith_et_al._1952 "bacillus cereus var. thuringiensis" smith et al. 1952]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EA2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EA2 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=INS:1,2,3,4,5,6-HEXAHYDROXY-CYCLOHEXANE'>INS</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=INS:1,2,3,4,5,6-HEXAHYDROXY-CYCLOHEXANE'>INS</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3ea1\|3ea1]], [[3ea3\|3ea3]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3ea1\|3ea1]], [[3ea3\|3ea3]]</div></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Phosphatidylinositol_diacylglycerol-lyase Phosphatidylinositol diacylglycerol-lyase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.6.1.13 4.6.1.13] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Phosphatidylinositol_diacylglycerol-lyase Phosphatidylinositol diacylglycerol-lyase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.6.1.13 4.6.1.13] </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=3ea2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ea2 OCA], [~~http~~://pdbe.org/3ea2 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3ea2 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3ea2 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3ea2 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=3ea2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ea2 OCA], [https://pdbe.org/3ea2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ea2 RCSB], [https://www.ebi.ac.uk/pdbsum/3ea2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ea2 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[~~http~~://www.uniprot.org/uniprot/PLC_BACTU PLC_BACTU]] Cleaves glycosylphosphatidylinositol (GPI) and phosphatidylinositol (PI) anchors but not PI phosphates.		[[https://www.uniprot.org/uniprot/PLC_BACTU PLC_BACTU]] Cleaves glycosylphosphatidylinositol (GPI) and phosphatidylinositol (PI) anchors but not PI phosphates.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 08:01, 31 July 2019

2019-07-31T08:01:50Z

← Older revision		Revision as of 08:01, 31 July 2019
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	==Crystal Structure of the Myo-inositol bound Y247S/Y251S Mutant of Phosphatidylinositol-Specific Phospholipase C from Bacillus Thuringiensis==		==Crystal Structure of the Myo-inositol bound Y247S/Y251S Mutant of Phosphatidylinositol-Specific Phospholipase C from Bacillus Thuringiensis==
	<StructureSection load='3ea2' size='340' side='right' caption='[[3ea2]], [[Resolution\|resolution]] 1.95Å' scene=''>		<StructureSection load='3ea2' size='340' side='right'caption='[[3ea2]], [[Resolution\|resolution]] 1.95Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3ea2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_cereus_var._thuringiensis"_smith_et_al._1952 "bacillus cereus var. thuringiensis" smith et al. 1952]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EA2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3EA2 FirstGlance]. <br>		<table><tr><td colspan='2'>[[3ea2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_cereus_var._thuringiensis"_smith_et_al._1952 "bacillus cereus var. thuringiensis" smith et al. 1952]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EA2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3EA2 FirstGlance]. <br>
Line 15:		Line 15:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ea/3ea2_consurf.spt"</scriptWhenChecked>		<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ea/3ea2_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>
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	</div>		</div>
	<div class="pdbe-citations 3ea2" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 3ea2" style="background-color:#fffaf0;"></div>

			==See Also==
			*[[Phospholipase C\|Phospholipase C]]
	== References ==		== References ==
	<references/>		<references/>
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	</StructureSection>		</StructureSection>
	[[Category: Bacillus cereus var. thuringiensis smith et al. 1952]]		[[Category: Bacillus cereus var. thuringiensis smith et al. 1952]]
			[[Category: Large Structures]]
	[[Category: Phosphatidylinositol diacylglycerol-lyase]]		[[Category: Phosphatidylinositol diacylglycerol-lyase]]
	[[Category: Head, J F]]		[[Category: Head, J F]]

OCA at 09:06, 25 October 2017

2017-10-25T09:06:50Z

← Older revision		Revision as of 09:06, 25 October 2017
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	==Crystal Structure of the Myo-inositol bound Y247S/Y251S Mutant of Phosphatidylinositol-Specific Phospholipase C from Bacillus Thuringiensis==		==Crystal Structure of the Myo-inositol bound Y247S/Y251S Mutant of Phosphatidylinositol-Specific Phospholipase C from Bacillus Thuringiensis==
	<StructureSection load='3ea2' size='340' side='right' caption='[[3ea2]], [[Resolution\|resolution]] 1.95Å' scene=''>		<StructureSection load='3ea2' size='340' side='right' caption='[[3ea2]], [[Resolution\|resolution]] 1.95Å' scene=''>
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	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3ea1\|3ea1]], [[3ea3\|3ea3]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3ea1\|3ea1]], [[3ea3\|3ea3]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphatidylinositol_diacylglycerol-lyase Phosphatidylinositol diacylglycerol-lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.6.1.13 4.6.1.13] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphatidylinositol_diacylglycerol-lyase Phosphatidylinositol diacylglycerol-lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.6.1.13 4.6.1.13] </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=3ea2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ea2 OCA], [http://pdbe.org/3ea2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ea2 RCSB], [http://www.ebi.ac.uk/pdbsum/3ea2 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=3ea2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ea2 OCA], [http://pdbe.org/3ea2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ea2 RCSB], [http://www.ebi.ac.uk/pdbsum/3ea2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ea2 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 29:		Line 30:
	</div>		</div>
	<div class="pdbe-citations 3ea2" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 3ea2" style="background-color:#fffaf0;"></div>

	~~==See Also==~~
	*[[Phospholipase C\|Phospholipase C]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 22:38, 8 February 2016

2016-02-08T22:38:55Z

← Older revision		Revision as of 22:38, 8 February 2016
Line 2:		Line 2:
	<StructureSection load='3ea2' size='340' side='right' caption='[[3ea2]], [[Resolution\|resolution]] 1.95Å' scene=''>		<StructureSection load='3ea2' size='340' side='right' caption='[[3ea2]], [[Resolution\|resolution]] 1.95Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3ea2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Bacillus_thuringiensis Bacillus~~ thuringiensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EA2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3EA2 FirstGlance]. <br>		<table><tr><td colspan='2'>[[3ea2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_cereus_var._thuringiensis"_smith_et_al._1952 "bacillus cereus var. thuringiensis" smith et al. 1952]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EA2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3EA2 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=INS:1,2,3,4,5,6-HEXAHYDROXY-CYCLOHEXANE'>INS</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=INS:1,2,3,4,5,6-HEXAHYDROXY-CYCLOHEXANE'>INS</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3ea1\|3ea1]], [[3ea3\|3ea3]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3ea1\|3ea1]], [[3ea3\|3ea3]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphatidylinositol_diacylglycerol-lyase Phosphatidylinositol diacylglycerol-lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.6.1.13 4.6.1.13] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphatidylinositol_diacylglycerol-lyase Phosphatidylinositol diacylglycerol-lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.6.1.13 4.6.1.13] </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=3ea2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ea2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ea2 RCSB], [http://www.ebi.ac.uk/pdbsum/3ea2 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=3ea2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ea2 OCA], [http://pdbe.org/3ea2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ea2 RCSB], [http://www.ebi.ac.uk/pdbsum/3ea2 PDBsum]</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=3ea2 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
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 3ea2" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[~~Phosphatidylinositol-specific phospholipase~~ C\|~~Phosphatidylinositol-specific phospholipase~~ C]]		*[[Phospholipase C\|Phospholipase C]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Bacillus thuringiensis]]		[[Category: Bacillus cereus var. thuringiensis smith et al. 1952]]
	[[Category: Phosphatidylinositol diacylglycerol-lyase]]		[[Category: Phosphatidylinositol diacylglycerol-lyase]]
	[[Category: Head, J F]]		[[Category: Head, J F]]

OCA at 02:36, 25 December 2014

2014-12-25T02:36:56Z

← Older revision		Revision as of 02:36, 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=3ea2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ea2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ea2 RCSB], [http://www.ebi.ac.uk/pdbsum/3ea2 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=3ea2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ea2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ea2 RCSB], [http://www.ebi.ac.uk/pdbsum/3ea2 PDBsum]</span></td></tr>
	</table>		</table>
			== Function ==
			[[http://www.uniprot.org/uniprot/PLC_BACTU PLC_BACTU]] Cleaves glycosylphosphatidylinositol (GPI) and phosphatidylinositol (PI) anchors but not PI phosphates.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 13:36, 19 November 2014

2014-11-19T13:36:34Z

← Older revision		Revision as of 13:36, 19 November 2014
Line 1:		Line 1:
	[[Image:~~3ea2~~.~~png~~\|~~left~~\|~~200px~~]]		==Crystal Structure of the Myo-inositol bound Y247S/Y251S Mutant of Phosphatidylinositol-Specific Phospholipase C from Bacillus Thuringiensis==
			<StructureSection load='3ea2' size='340' side='right' caption='[[3ea2]], [[Resolution\|resolution]] 1.95Å' scene=''>
			== Structural highlights ==
			<table><tr><td colspan='2'>[[3ea2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_thuringiensis Bacillus thuringiensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EA2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3EA2 FirstGlance]. <br>
			</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=INS:1,2,3,4,5,6-HEXAHYDROXY-CYCLOHEXANE'>INS</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
			<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3ea1\|3ea1]], [[3ea3\|3ea3]]</td></tr>
			<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphatidylinositol_diacylglycerol-lyase Phosphatidylinositol diacylglycerol-lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.6.1.13 4.6.1.13] </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=3ea2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ea2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ea2 RCSB], [http://www.ebi.ac.uk/pdbsum/3ea2 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/ea/3ea2_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 ==
			Cleavage of phosphatidylinositol (PI) to inositol 1,2-(cyclic)-phosphate (cIP) and cIP hydrolysis to inositol 1-phosphate by Bacillus thuringiensis phosphatidylinositol-specific phospholipase C are activated by the enzyme binding to phosphatidylcholine (PC) surfaces. Part of this reflects improved binding of the protein to interfaces. However, crystallographic analysis of an interfacially impaired phosphatidylinositol-specific phospholipase (W47A/W242A) suggested protein dimerization might occur on the membrane. In the W47A/W242A dimer, four tyrosine residues from one monomer interact with the same tyrosine cluster of the other, forming a tight dimer interface close to the membrane binding regions. We have constructed mutant proteins in which two or more of these tyrosine residues have been replaced with serine. Phospholipid binding and enzymatic activity of these mutants have been examined to assess the importance of these residues to enzyme function. Replacing two tyrosines had small effects on enzyme activity. However, removal of three or four tyrosine residues weakened PC binding and reduced PI cleavage by the enzyme as well as PC activation of cIP hydrolysis. Crystal structures of Y247S/Y251S in the absence and presence of myo-inositol as well as Y246S/Y247S/Y248S/Y251S indicate that both mutant proteins crystallized as monomers, were very similar to one another, and had no change in the active site region. Kinetic assays, lipid binding, and structural results indicate that either (i) a specific PC binding site, critical for vesicle activities and cIP activation, has been impaired, or (ii) the reduced dimerization potential for Y246S/Y247S/Y248S and Y246S/Y247S/Y248S/Y251S is responsible for their reduced catalytic activity in all assay systems.

	~~{{STRUCTURE_3ea2\| PDB=3ea2 \| SCENE= }}~~		Modulation of Bacillus thuringiensis phosphatidylinositol-specific phospholipase C activity by mutations in the putative dimerization interface.,Shi X, Shao C, Zhang X, Zambonelli C, Redfield AG, Head JF, Seaton BA, Roberts MF J Biol Chem. 2009 Jun 5;284(23):15607-18. Epub 2009 Apr 15. PMID:19369255<ref>PMID:19369255</ref>

	~~===Crystal Structure~~ of the ~~Myo-inositol bound Y247S~~/~~Y251S Mutant of Phosphatidylinositol-Specific Phospholipase C from Bacillus Thuringiensis===~~		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>

	~~{{ABSTRACT_PUBMED_19369255}}~~		==See Also==
			*[[Phosphatidylinositol-specific phospholipase C\|Phosphatidylinositol-specific phospholipase C]]
	==~~About this Structure~~==		== References ==
	[[~~3ea2~~]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_thuringiensis Bacillus thuringiensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EA2 OCA].		<references/>
			__TOC__
	==~~Reference~~==		</StructureSection>
	<~~ref group="xtra">PMID:019369255<~~/~~ref~~><~~references group="xtra"~~/>
	[[Category: Bacillus thuringiensis]]		[[Category: Bacillus thuringiensis]]
	[[Category: Phosphatidylinositol diacylglycerol-lyase]]		[[Category: Phosphatidylinositol diacylglycerol-lyase]]
	[[Category: Head, J F.]]		[[Category: Head, J F]]
	[[Category: Redfied, A G.]]		[[Category: Redfied, A G]]
	[[Category: Roberts, M F.]]		[[Category: Roberts, M F]]
	[[Category: Seaton, B A.]]		[[Category: Seaton, B A]]
	[[Category: Shao, C.]]		[[Category: Shao, C]]
	[[Category: Shi, X.]]		[[Category: Shi, X]]
	[[Category: Zambonelli, C.]]		[[Category: Zambonelli, C]]
	[[Category: Zhang, X.]]		[[Category: Zhang, X]]
	[[Category: Dimer]]		[[Category: Dimer]]
	[[Category: Interfacially impaired]]		[[Category: Interfacially impaired]]

OCA: Protected "3ea2" [edit=sysop:move=sysop]

2013-01-09T09:05:34Z

Protected "3ea2" [edit=sysop:move=sysop]

← Older revision	Revision as of 09:05, 9 January 2013
(No difference)

OCA at 09:05, 9 January 2013

2013-01-09T09:05:30Z

← Older revision		Revision as of 09:05, 9 January 2013
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	~~{{Seed}}~~
	[[Image:3ea2.png\|left\|200px]]		[[Image:3ea2.png\|left\|200px]]

	~~<!--~~
	~~The line below this paragraph, containing "STRUCTURE_3ea2", 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_3ea2\| PDB=3ea2 \| SCENE= }}		{{STRUCTURE_3ea2\| PDB=3ea2 \| SCENE= }}

	===Crystal Structure of the Myo-inositol bound Y247S/Y251S Mutant of Phosphatidylinositol-Specific Phospholipase C from Bacillus Thuringiensis===		===Crystal Structure of the Myo-inositol bound Y247S/Y251S Mutant of Phosphatidylinositol-Specific Phospholipase C from Bacillus Thuringiensis===

			{{ABSTRACT_PUBMED_19369255}}

	==About this Structure==		==About this Structure==
	~~3EA2~~ is a 2 ~~chains~~ structure ~~of sequences~~ from [http://en.wikipedia.org/wiki/Bacillus_thuringiensis Bacillus thuringiensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EA2 OCA].		[[3ea2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_thuringiensis Bacillus thuringiensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EA2 OCA].

			==Reference==
			<ref group="xtra">PMID:019369255</ref><references group="xtra"/>
	[[Category: Bacillus thuringiensis]]		[[Category: Bacillus thuringiensis]]
	[[Category: Phosphatidylinositol diacylglycerol-lyase]]		[[Category: Phosphatidylinositol diacylglycerol-lyase]]
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	[[Category: Secreted]]		[[Category: Secreted]]
	[[Category: Tim barrel]]		[[Category: Tim barrel]]

	~~''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 10 22:20:21 2009''~~

OCA at 19:16, 10 June 2009

2009-06-10T19:16:11Z

← Older revision		Revision as of 19:16, 10 June 2009
Line 12:		Line 12:
	===Crystal Structure of the Myo-inositol bound Y247S/Y251S Mutant of Phosphatidylinositol-Specific Phospholipase C from Bacillus Thuringiensis===		===Crystal Structure of the Myo-inositol bound Y247S/Y251S Mutant of Phosphatidylinositol-Specific Phospholipase C from Bacillus Thuringiensis===


	~~<!--~~
	~~The line below this paragraph, {{ABSTRACT_PUBMED_19369255}}, adds the Publication Abstract to the page~~
	~~(as it appears on PubMed at http://www.pubmed.gov), where 19369255 is the PubMed ID number.~~
	~~-->~~
	~~{{ABSTRACT_PUBMED_19369255}}~~

	==About this Structure==		==About this Structure==
	3EA2 is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Bacillus_thuringiensis Bacillus thuringiensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EA2 OCA].		3EA2 is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Bacillus_thuringiensis Bacillus thuringiensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EA2 OCA].

	~~==Reference==~~
	~~<ref group="xtra">PMID:19369255</ref><references group="xtra"/>~~
	[[Category: Bacillus thuringiensis]]		[[Category: Bacillus thuringiensis]]
	[[Category: Phosphatidylinositol diacylglycerol-lyase]]		[[Category: Phosphatidylinositol diacylglycerol-lyase]]
Line 45:		Line 36:
	[[Category: Tim barrel]]		[[Category: Tim barrel]]

	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 10 18:20:33 2009''		''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 10 22:20:21 2009''