1ptd
From Proteopedia
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| - | [[Image:1ptd.jpg|left|200px]] | + | [[Image:1ptd.jpg|left|200px]] |
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| - | '''PHOSPHATIDYLINOSITOL-SPECIFIC PHOSPHOLIPASE C''' | + | {{Structure |
| + | |PDB= 1ptd |SIZE=350|CAPTION= <scene name='initialview01'>1ptd</scene>, resolution 2.6Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |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] | ||
| + | |GENE= PI-PLC GENE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1396 Bacillus cereus]) | ||
| + | }} | ||
| + | |||
| + | '''PHOSPHATIDYLINOSITOL-SPECIFIC PHOSPHOLIPASE C''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1PTD is a [ | + | 1PTD is a [[Single protein]] structure of sequence from [http://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]. |
==Reference== | ==Reference== | ||
| - | 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:// | + | 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://www.ncbi.nlm.nih.gov/pubmed/7664726 7664726] |
[[Category: Bacillus cereus]] | [[Category: Bacillus cereus]] | ||
[[Category: Phosphatidylinositol diacylglycerol-lyase]] | [[Category: Phosphatidylinositol diacylglycerol-lyase]] | ||
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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 Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:28:44 2008'' |
Revision as of 11:28, 20 March 2008
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| , resolution 2.6Å | |||||||
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| Gene: | PI-PLC GENE (Bacillus cereus) | ||||||
| Activity: | Phosphatidylinositol diacylglycerol-lyase, with EC number 4.6.1.13 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
PHOSPHATIDYLINOSITOL-SPECIFIC PHOSPHOLIPASE C
Overview
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 Structure
1PTD is a Single protein structure of sequence from Bacillus cereus. Full crystallographic information is available from OCA.
Reference
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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