C2 domain conformational changes in phospholipase C-delta 1.
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.
Grobler
J A
JA
Laboratory of Molecular Biology, National Institute of Diabetes, Digestive, and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892-0580, USA.
Essen
L O
LO
Williams
R L
RL
Hurley
J H
JH
D000818:Animals; D001051:Apoenzymes / Q000737:chemistry; D001665:Binding Sites; D002118:Calcium / Q000378:metabolism; D018360:Crystallography, X-Ray; D007527:Isoenzymes / Q000737:chemistry* / Q000378:metabolism; D008239:Lysine; D008958:Models, Molecular; D054803:Phospholipase C delta; D011487:Protein Conformation; D051381:Rats; D012493:Samarium / Q000378:metabolism; D010738:Type C Phospholipases / Q000737:chemistry* / Q000378:metabolism
D001051:Apoenzymes; D007527:Isoenzymes; D012493:Samarium; D010738:Type C Phospholipases; D054803:Phospholipase C delta; D008239:Lysine; D002118:Calcium