2plc: Difference between revisions

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-{{Seed}}
-[[Image:2plc.png|left|200px]]
-<!--
+==PHOSPHATIDYLINOSITOL-SPECIFIC PHOSPHOLIPASE C FROM LISTERIA MONOCYTOGENES==
-The line below this paragraph, containing "STRUCTURE_2plc", creates the "Structure Box" on the page.
+<StructureSection load='2plc' size='340' side='right'caption='[[2plc]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[2plc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Listeria_monocytogenes Listeria monocytogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PLC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PLC FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</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&#8491;</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=2plc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2plc OCA], [https://pdbe.org/2plc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2plc RCSB], [https://www.ebi.ac.uk/pdbsum/2plc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2plc ProSAT]</span></td></tr>
-{{STRUCTURE_2plc|  PDB=2plc  |  SCENE=  }}
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/PLC_LISMO PLC_LISMO] Cleaves glycosylphosphatidylinositol (GPI) and phosphatidylinositol (PI) anchors but not PI phosphates. Important factor in pathogenesis, PI-PLC activity is present only in virulent listeria species. It may participate in the lysis of the phagolysosomal membrane.
+== 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/pl/2plc_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/main_output.php?pdb_ID=2plc ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The X-ray crystal structure of the phosphatidylinositol-specific phospholipase C (PI-PLC) from the human pathogen Listeria monocytogenes has been determined both in free form at 2.0 A resolution, and in complex with the competitive inhibitor myo-inositol at 2.6 A resolution. The structure was solved by a combination of molecular replacement using the structure of Bacillus cereus PI-PLC and single isomorphous replacement. The enzyme consists of a single (beta alpha)8-barrel domain with the active site located at the C-terminal side of the beta-barrel. Unlike other (beta alpha)8-barrels, the barrel in PI-PLC is open because it lacks hydrogen bonding interactions between beta-strands V and VI. myo-Inositol binds to the active site pocket by making specific hydrogen bonding interactions with a number of charged amino acid side-chains as well as a coplanar stacking interaction with a tyrosine residue. Despite a relatively low sequence identity of approximately 24%, the structure is highly homologous to that of B.cereus PI-PLC with an r.m.s. deviation for 228 common C alpha positions of 1.46 A. Larger differences are found for loop regions that accommodate most of the numerous amino acid insertions and deletions. The active site pocket is also well conserved with only two amino acid replacements directly implicated in inositol binding.
-===PHOSPHATIDYLINOSITOL-SPECIFIC PHOSPHOLIPASE C FROM LISTERIA MONOCYTOGENES===
+Crystal structure of the phosphatidylinositol-specific phospholipase C from the human pathogen Listeria monocytogenes.,Moser J, Gerstel B, Meyer JE, Chakraborty T, Wehland J, Heinz DW J Mol Biol. 1997 Oct 17;273(1):269-82. PMID:9367761<ref>PMID:9367761</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2plc" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_9367761}}, adds the Publication Abstract to the page
+*[[Phospholipase C|Phospholipase C]]
-(as it appears on PubMed at http://www.pubmed.gov), where 9367761 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_9367761}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Large Structures]]
-PLC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Listeria_monocytogenes Listeria monocytogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PLC OCA].
-==Reference==
-Crystal structure of the phosphatidylinositol-specific phospholipase C from the human pathogen Listeria monocytogenes., Moser J, Gerstel B, Meyer JE, Chakraborty T, Wehland J, Heinz DW, J Mol Biol. 1997 Oct 17;273(1):269-82. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9367761 9367761]
 [[Category: Listeria monocytogenes]]
-[[Category: Phosphatidylinositol diacylglycerol-lyase]]
+[[Category: Heinz DW]]
-[[Category: Single protein]]
+[[Category: Moser J]]
-[[Category: Heinz, D W.]]
-[[Category: Moser, J.]]
-[[Category: Hydrolase]]
-[[Category: Phospholipid degradation]]
-[[Category: Virulence factor of human pathogen]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 17:09:07 2008''