C2 domain conformational changes in phospholipase C-delta 1

Nat Struct Biol. 1996 Sep;3(9):788-95. doi: 10.1038/nsb0996-788.


The structure of the PH-domain truncated core of rat phosphoinositide-specific phospholipase C-delta 1 has been determined at 2.4 A resolution and compared to the structure previously determined in a different crystal form. The stereochemical relationship between the EF, catalytic, and C2 domains is essentially identical. The Ca2+ analogue Sm3+ binds at two sites between the jaws of the C2 domain. Sm3+ binding ejects three lysine residues which bridge the gap between the jaws and occupy the Ca2+ site in the apoenzyme, triggering a conformational change in the jaws. The distal sections of the C2 jaws move apart, opening the mouth by 9 A and creating a gap large enough to bind a phospholipid headgroup.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Apoenzymes / chemistry
  • Binding Sites
  • Calcium / metabolism
  • Crystallography, X-Ray
  • Isoenzymes / chemistry*
  • Isoenzymes / metabolism
  • Lysine
  • Models, Molecular
  • Phospholipase C delta
  • Protein Conformation*
  • Rats
  • Samarium / metabolism
  • Type C Phospholipases / chemistry*
  • Type C Phospholipases / metabolism


  • Apoenzymes
  • Isoenzymes
  • Samarium
  • Type C Phospholipases
  • Phospholipase C delta
  • Lysine
  • Calcium