2b96

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Revision as of 06:31, 21 November 2007

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spinqualitylabelsall models 2b96, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Third Calcium ion found in an inhibitor bound phospholipase A2

Overview

The lipolytic enzyme phospholipase A2 plays a crucial role in lipid, metabolism and catalyzes hydrolysis of the fatty-acid ester bond at the, sn-2 position of phospholipids. Here, the crystal structure (1.7 A, resolution) of the triple mutant (K53,56,121M) of bovine pancreatic, phospholipase A2 complexed with an organic molecule, p-methoxybenzoic acid, (anisic acid), is reported. Residues 60-70 (the surface-loop residues) are, ordered and adopt conformations which are different from those normally, found in structures in which a second calcium ion is present. It is, interesting to note that for the first time a third calcium ion has been, identified. In addition, four Tris, (2-amino-2-hydroxymethyl-1,3-propanediol) molecules were located. It is, believed that one of the Tris molecules plays a role in clamping the third, calcium ion and that another is involved in controlling the dynamics of, the surface loop through hydrogen bonds.

About this Structure

2B96 is a Single protein structure of sequence from Bos taurus with CA, CL, TRS and ANN as ligands. Active as Phospholipase A(2), with EC number 3.1.1.4 Full crystallographic information is available from OCA.

Reference

Third calcium ion found in an inhibitor-bound phospholipase A2., Sekar K, Gayathri D, Velmurugan D, Jeyakanthan J, Yamane T, Poi MJ, Tsai MD, Acta Crystallogr D Biol Crystallogr. 2006 Apr;62(Pt 4):392-7. Epub 2006, Mar 18. PMID:16552140

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