2b96
From Proteopedia
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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 , , and 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
Page seeded by OCA on Thu Feb 21 16:35:23 2008
Categories: Bos taurus | Phospholipase A(2) | Single protein | Sekar, K. | Tsai, M D. | Velmurugan, D. | Yamane, T. | ANN | CA | CL | TRS | Alpha helix | Anisic acid | Beta sheet | Triple mutant
