Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
