2B96
Third Calcium ion found in an inhibitor bound phospholipase A2
Summary for 2B96
| Entry DOI | 10.2210/pdb2b96/pdb |
| Related | 1mkt 1une |
| Descriptor | Phospholipase A2, CALCIUM ION, CHLORIDE ION, ... (6 entities in total) |
| Functional Keywords | alpha helix, beta sheet, triple mutant, anisic acid, hydrolase |
| Biological source | Bos taurus (cattle) |
| Cellular location | Secreted: P00593 |
| Total number of polymer chains | 1 |
| Total formula weight | 14612.96 |
| Authors | Sekar, K.,Velmurugan, D.,Yamane, T.,Tsai, M.D. (deposition date: 2005-10-11, release date: 2006-03-28, Last modification date: 2024-10-30) |
| Primary citation | Sekar, K.,Gayathri, D.,Velmurugan, D.,Jeyakanthan, J.,Yamane, T.,Poi, M.J.,Tsai, M.D. Third Calcium ion found in an inhibitor bound phospholipase A2 Acta Crystallogr.,Sect.D, 62:392-397, 2006 Cited by PubMed Abstract: 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. PubMed: 16552140DOI: 10.1107/S0907444906001612 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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