1ptd: Difference between revisions

Revision as of 05:28, 3 May 2008

PHOSPHATIDYLINOSITOL-SPECIFIC PHOSPHOLIPASE C

OverviewOverview

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.

About this StructureAbout this Structure

1PTD is a Single protein structure of sequence from Bacillus cereus. Full crystallographic information is available from OCA.

ReferenceReference

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:7664726 Page seeded by OCA on Sat May 3 05:27:59 2008

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OCA

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 [[Image:1ptd.jpg|left|200px]]
- {{Structure
+<!--
-|PDB= 1ptd |SIZE=350|CAPTION= <scene name='initialview01'>1ptd</scene>, resolution 2.6&Aring;
+The line below this paragraph, containing "STRUCTURE_1ptd", creates the "Structure Box" on the page.
-|SITE=
+You may change the PDB parameter (which sets the PDB file loaded into the applet)
-|LIGAND=
+or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-|ACTIVITY= <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>
+or leave the SCENE parameter empty for the default display.
-|GENE= PI-PLC GENE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1396 Bacillus cereus])
+-->
-|DOMAIN=
+{{STRUCTURE_1ptd|  PDB=1ptd  |  SCENE=  }}
-|RELATEDENTRY=
-|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ptd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ptd OCA], [http://www.ebi.ac.uk/pdbsum/1ptd PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ptd RCSB]</span>
-}}
 '''PHOSPHATIDYLINOSITOL-SPECIFIC PHOSPHOLIPASE C'''
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 [[Category: Heinz, D W.]]
 [[Category: Ryan, M.]]
-[[Category: hydrolase]]
+[[Category: Hydrolase]]
-[[Category: phosphatidylinositol specific phospholipase c]]
+[[Category: Phosphatidylinositol specific phospholipase c]]
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 05:27:59 2008''
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:04:17 2008''