1ptg

<StructureSection load='1ptg' size='340' side='right' caption='[[1ptg]], [[Resolution|resolution]] 2.60&Aring;' scene=''>

<table><tr><td colspan='2'>[[1ptg]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_14579 Atcc 14579]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PTG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PTG 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></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PI-PLC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1396 ATCC 14579])</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=1ptg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ptg OCA], [http://pdbe.org/1ptg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ptg RCSB], [http://www.ebi.ac.uk/pdbsum/1ptg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ptg ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/PLC_BACCE PLC_BACCE]] Cleaves glycosylphosphatidylinositol (GPI) and phosphatidylinositol (PI) anchors but not PI phosphates.

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== Publication Abstract from PubMed ==

Phosphatidylinositol (PI), once regarded as an obscure component of membranes, is now recognized as an important reservoir of second messenger precursors and as an anchor for membrane enzymes. PI-specific phospholipase C (PI-PLC) is the enzyme that cleaves PI, invoking numerous cellular responses. The crystal structure of PI-PLC from Bacillus cereus (EC 3.1.4.10) has been solved at 2.6 A resolution and refined to a crystallographic R factor of 18.7%. The structure consists of an imperfect (beta alpha)8-barrel similar to that first observed for triose phosphate isomerase and does not resemble any other known phospholipase structure. The active site of the enzyme has been identified by determining the structure of PI-PLC in complex with its inhibitor, myo-inositol, at 2.6 A resolution (R factor = 19.5%). This substrate-like inhibitor interacts with a number of residues highly conserved among prokaryotic PI-PLCs. Residues His32 and His82, which are also conserved between prokaryotic and eukaryotic PI-PLCs, most likely act as general base and acid respectively in a catalytic mechanism analogous to that observed for ribonucleases.

 

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== References ==

[[Category: Atcc 14579]]

[[Category: Phosphatidylinositol diacylglycerol-lyase]]

[[Category: Bullock, T L]]

[[Category: Griffith, O H]]

[[Category: Heinz, D W]]

[[Category: Ryan, M]]

[[Category: Phosphatidylinositol specific phospholipase c]]