Crystal structure of a mammalian phosphoinositide-specific phospholipase C delta

Nature. 1996 Apr 18;380(6575):595-602. doi: 10.1038/380595a0.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Catalysis
  • Cell Membrane / metabolism
  • Crystallography, X-Ray
  • Humans
  • Hydrolysis
  • Inositol 1,4,5-Trisphosphate / metabolism
  • Isoenzymes / chemistry*
  • Isoenzymes / metabolism
  • Models, Molecular
  • Molecular Conformation
  • Molecular Sequence Data
  • Phosphoinositide Phospholipase C
  • Phospholipase C delta
  • Phosphoric Diester Hydrolases / chemistry*
  • Phosphoric Diester Hydrolases / metabolism
  • Protein Binding
  • Protein Conformation
  • Rats
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / metabolism
  • Second Messenger Systems
  • Sequence Homology, Amino Acid

Substances

  • Isoenzymes
  • Recombinant Proteins
  • Inositol 1,4,5-Trisphosphate
  • Phosphoric Diester Hydrolases
  • Phosphoinositide Phospholipase C
  • Phospholipase C delta