2isd
From Proteopedia
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|PDB= 2isd |SIZE=350|CAPTION= <scene name='initialview01'>2isd</scene>, resolution 2.5Å | |PDB= 2isd |SIZE=350|CAPTION= <scene name='initialview01'>2isd</scene>, resolution 2.5Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ACT:ACETATE ION'>ACT</scene> | + | |LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Phosphoinositide_phospholipase_C Phosphoinositide phospholipase C], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.4.11 3.1.4.11] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoinositide_phospholipase_C Phosphoinositide phospholipase C], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.4.11 3.1.4.11] </span> |
|GENE= CDNA FRAGMENT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus]) | |GENE= CDNA FRAGMENT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2isd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2isd OCA], [http://www.ebi.ac.uk/pdbsum/2isd PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2isd RCSB]</span> | ||
}} | }} | ||
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[[Category: Perisic, O.]] | [[Category: Perisic, O.]] | ||
[[Category: Williams, R L.]] | [[Category: Williams, R L.]] | ||
| - | [[Category: ACT]] | ||
[[Category: calcium-binding]] | [[Category: calcium-binding]] | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
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[[Category: transducer]] | [[Category: transducer]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:47:50 2008'' |
Revision as of 00:47, 31 March 2008
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| , resolution 2.5Å | |||||||
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| Ligands: | |||||||
| Gene: | CDNA FRAGMENT (Rattus norvegicus) | ||||||
| Activity: | Phosphoinositide phospholipase C, with EC number 3.1.4.11 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C-DELTA1 FROM RAT
Overview
Mammalian phosphoinositide-specific phospholipase C enzymes (PI-PLC) act as signal transducers that generate two second messengers, inositol-1,4,5-trisphosphate and diacylglycerol. The 2.4-A structure of phospholipase C delta 1 reveals a multidomain protein incorporating modules shared by many signalling proteins. The structure suggests a mechanism for membrane attachment and Ca2+-dependent hydrolysis of second-messenger precursors. The regulation and reversible membrane association of PI-PLC may serve as a model for understanding other multidomain enzymes involved in phospholipid signalling.
About this Structure
2ISD is a Single protein structure of sequence from Rattus norvegicus. This structure supersedes the now removed PDB entry 1ISD. Full crystallographic information is available from OCA.
Reference
Crystal structure of a mammalian phosphoinositide-specific phospholipase C delta., Essen LO, Perisic O, Cheung R, Katan M, Williams RL, Nature. 1996 Apr 18;380(6575):595-602. PMID:8602259
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