1QAS

1-PHOSPHATIDYLINOSITOL-4,5-BISPHOSPHATE PHOSPHODIESTERASE DELTA 1

Summary for 1QAS

• Entry DOI: 10.2210/pdb1qas/pdb
• Descriptor: PHOSPHOLIPASE C DELTA-1 (2 entities in total)
• Functional Keywords: hydrolase, lipid degradation, transducer, calcium-binding
• Biological source: Rattus norvegicus (Norway rat)
• Total number of polymer chains: 2
• Total formula weight: 140860.77

Authors

Grobler, J.A.,Hurley, J.H. (deposition date: 1996-08-02, release date: 1997-02-12, Last modification date: 2024-04-03)

Primary citation

Grobler, J.A.,Essen, L.O.,Williams, R.L.,Hurley, J.H.
C2 domain conformational changes in phospholipase C-delta 1.
Nat.Struct.Biol., 3:788-795, 1996

PubMed Abstract: 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.

PubMed: 8784353
DOI: 10.1038/nsb0996-788

Experimental method

X-RAY DIFFRACTION (2.4 Å)