2ZP5
Carboxylic ester hydrolase, single mutant d49k of bovine pancreatic pla2 enzyme
Summary for 2ZP5
| Entry DOI | 10.2210/pdb2zp5/pdb |
| Related | 2ZP3 2ZP4 |
| Descriptor | Phospholipase A2, CALCIUM ION, CHLORIDE ION, ... (4 entities in total) |
| Functional Keywords | hydrolase, active site mutant, metal binding protein, calcium, lipid degradation, metal-binding, pyrrolidone carboxylic acid, secreted |
| Biological source | Bos taurus (bovine,cow,domestic cattle,domestic cow) |
| Cellular location | Secreted: P00593 |
| Total number of polymer chains | 1 |
| Total formula weight | 13900.13 |
| Authors | Kanaujia, S.P.,Sekar, K. (deposition date: 2008-06-27, release date: 2008-11-04, Last modification date: 2024-10-23) |
| Primary citation | Kanaujia, S.P.,Sekar, K. Structures and molecular-dynamics studies of three active-site mutants of bovine pancreatic phospholipase A(2) Acta Crystallogr.,Sect.D, 64:1003-1011, 2008 Cited by PubMed Abstract: Phospholipase A(2) hydrolyzes phospholipids at the sn-2 position to cleave the fatty-acid ester bond of L-glycerophospholipids. The catalytic dyad (Asp99 and His48) along with a nucleophilic water molecule is responsible for enzyme hydrolysis. Furthermore, the residue Asp49 in the calcium-binding loop is essential for controlling the binding of the calcium ion and the catalytic action of phospholipase A(2). To elucidate the structural role of His48 and Asp49, the crystal structures of three active-site single mutants H48N, D49N and D49K have been determined at 1.9 A resolution. Although the catalytically important calcium ion is present in the H48N mutant, the crystal structure shows that proton transfer is not possible from the catalytic water to the mutated residue. In the case of the Asp49 mutants, no calcium ion was found in the active site. However, the tertiary structures of the three active-site mutants are similar to that of the trigonal recombinant enzyme. Molecular-dynamics simulation studies provide a good explanation for the crystallographic results. PubMed: 18931407DOI: 10.1107/S0907444908022713 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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