Acta Crystallographica Section D

Biological Crystallography

Volume 55, Part 2 (February 1999)

research papers

Acta Cryst. (1999). D55, 443-447 [ doi:10.1107/S0907444998013699 ]

Structures of the catalytic site mutants D99A and H48Q and the calcium-loop mutant D49E of phospholipase A₂

K. Sekar, R. Biswas, Y. Li, M.-D. Tsai and M. Sundaralingam

Abstract: Crystal structures of the active-site mutants D99A and H48Q and the calcium-loop mutant D49E of bovine phospholipase A₂ have been determined at around 1.9 Å resolution. The D99A mutant is isomorphous to the orthorhombic recombinant enzyme, space group P2₁2₁2₁. The H48Q and the calcium-loop mutant D49E are isomorphous to the trigonal recombinant enzyme, space group P3₁21. The two active-site mutants show no major structural perturbations. The structural water is absent in D99A and, therefore, the hydrogen-bonding scheme is changed. In H48Q, the catalytic water is present and hydrogen bonded to Gln48 N, but the second water found in native His48 is absent. In the calcium-loop mutant D49E, the two water molecules forming the pentagonal bipyramid around calcium are absent and only one O atom of the Glu49 carboxylate group is coordinated to calcium, resulting in only four ligands.

PDB references: 1kvx, 1kvy and 1kvw

Keywords: phospholipase A₂.

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