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1ptd

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(New page: 200px<br /><applet load="1ptd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ptd, resolution 2.6&Aring;" /> '''PHOSPHATIDYLINOSITOL-...)
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[[Image:1ptd.jpg|left|200px]]<br /><applet load="1ptd" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1ptd, resolution 2.6&Aring;" />
 
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'''PHOSPHATIDYLINOSITOL-SPECIFIC PHOSPHOLIPASE C'''<br />
 
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==Overview==
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==PHOSPHATIDYLINOSITOL-SPECIFIC PHOSPHOLIPASE C==
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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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<StructureSection load='1ptd' size='340' side='right'caption='[[1ptd]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1ptd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_cereus Bacillus cereus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PTD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PTD FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ptd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ptd OCA], [https://pdbe.org/1ptd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ptd RCSB], [https://www.ebi.ac.uk/pdbsum/1ptd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ptd ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PLC_BACCE PLC_BACCE] Cleaves glycosylphosphatidylinositol (GPI) and phosphatidylinositol (PI) anchors but not PI phosphates.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pt/1ptd_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1ptd ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1PTD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_cereus Bacillus cereus]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PTD OCA].
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*[[Phospholipase C|Phospholipase C]]
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__TOC__
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==Reference==
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</StructureSection>
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Crystal structure of the phosphatidylinositol-specific phospholipase C from Bacillus cereus in complex with myo-inositol., Heinz DW, Ryan M, Bullock TL, Griffith OH, EMBO J. 1995 Aug 15;14(16):3855-63. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7664726 7664726]
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[[Category: Bacillus cereus]]
[[Category: Bacillus cereus]]
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[[Category: Phosphatidylinositol diacylglycerol-lyase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Bullock TL]]
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[[Category: Bullock, T.L.]]
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[[Category: Griffith OH]]
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[[Category: Griffith, O.H.]]
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[[Category: Heinz DW]]
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[[Category: Heinz, D.W.]]
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[[Category: Ryan M]]
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[[Category: Ryan, M.]]
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[[Category: hydrolase]]
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[[Category: phosphatidylinositol specific phospholipase c]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:06:35 2007''
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Current revision

PHOSPHATIDYLINOSITOL-SPECIFIC PHOSPHOLIPASE C

PDB ID 1ptd

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