C2 domain conformational changes in phospholipase C-delta 1.

J A Grobler; L O Essen; R L Williams; J H Hurley

doi:10.1038/nsb0996-788

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PubMed · 8784353

C2 domain conformational changes in phospholipase C-delta 1.

J A Grobler·L O Essen·R L Williams·J H Hurley

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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.

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Animals Apoenzymes Binding Sites Calcium Crystallography, X-Ray Isoenzymes Lysine Models, Molecular Phospholipase C delta Protein Conformation Rats Samarium Type C Phospholipases Journal Article Research Support, Non-U.S. Gov't

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J A Grobler, L O Essen, R L Williams, J H Hurley. 1996. C2 domain conformational changes in phospholipase C-delta 1.. https://doi.org/10.1038/nsb0996-788

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