1ptg: Difference between revisions
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|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=INS:1,2,3,4,5,6-HEXAHYDROXY-CYCLOHEXANE'>INS</scene> | |LIGAND= <scene name='pdbligand=INS:1,2,3,4,5,6-HEXAHYDROXY-CYCLOHEXANE'>INS</scene> | ||
|ACTIVITY= [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] | |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> | ||
|GENE= PI-PLC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1396 Bacillus cereus]) | |GENE= PI-PLC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1396 Bacillus cereus]) | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<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://www.ebi.ac.uk/pdbsum/1ptg PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ptg RCSB]</span> | |||
}} | }} | ||
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[[Category: Heinz, D W.]] | [[Category: Heinz, D W.]] | ||
[[Category: Ryan, M.]] | [[Category: Ryan, M.]] | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
[[Category: inhibitor complex]] | [[Category: inhibitor complex]] | ||
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[[Category: phosphatidylinositol specific phospholipase c]] | [[Category: phosphatidylinositol specific phospholipase c]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:04:25 2008'' | ||
Revision as of 23:04, 30 March 2008
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| , resolution 2.6Å | |||||||
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| Ligands: | |||||||
| Gene: | PI-PLC (Bacillus cereus) | ||||||
| Activity: | Phosphatidylinositol diacylglycerol-lyase, with EC number 4.6.1.13 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
PHOSPHATIDYLINOSITOL-SPECIFIC PHOSPHOLIPASE C IN COMPLEX WITH MYO-INOSITOL
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
1PTG 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
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