1qas

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(New page: 200px<br /><applet load="1qas" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qas, resolution 2.4&Aring;" /> '''1-PHOSPHATIDYLINOSITO...)
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Revision as of 22:25, 20 November 2007


1qas, resolution 2.4Å

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

Overview

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.

About this Structure

1QAS is a Single protein structure of sequence from Rattus norvegicus. Active as Phosphoinositide phospholipase C, with EC number 3.1.4.11 Full crystallographic information is available from OCA.

Reference

C2 domain conformational changes in phospholipase C-delta 1., Grobler JA, Essen LO, Williams RL, Hurley JH, Nat Struct Biol. 1996 Sep;3(9):788-95. PMID:8784353

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