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Atomic resolution (0.97 angstrom) structure of the triple mutant(K53,56,121M) of bovine pancreatic phospholipase $A_{2}$

Sekar, K and Rajakannan, V and Gayathri, D and Velmurugan, D and Poi, MJ and Dauter, M and Dauter, Z and Tsai, MD (2005) Atomic resolution (0.97 angstrom) structure of the triple mutant(K53,56,121M) of bovine pancreatic phospholipase $A_{2}$. In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 61 (Part 1). pp. 3-7.

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Abstract

The enzyme phospholipase $A_{2}$ catalyzes the hydrolysis of the sn-2 acyl chain of phospholipids, forming fatty acids and lysophospholipids. The crystal structure of a triple mutant (K53,56,121M) of bovine pancreatic phospholipase $A_{2}$ in which the lysine residues at positions 53, 56 and 121 are replaced recombinantly by methionines has been determined at atomic resolution (0.97 angstrom). The crystal is monoclinic (space group P2), with unit-cell parameters a = 36.934, b = 23.863, c = 65.931 angstrom, = 101.47 anstrom. The structure was solved by molecular replacement and has been refined to a final R factor of 10.6% ($R_{free}$ = 13.4%) using 63 926 unique reflections. The final protein model consists of 123 amino-acid residues, two calcium ions, one chloride ion, 243 water molecules and six 2-methyl-2,4-pentanediol molecules. The surface-loop residues 60-70 are ordered and have clear electron density.

Item Type: Journal Article
Additional Information: Copyright for this article belongs to Blackwell Publishing.
Keywords: phospholipase A2
Department/Centre: Division of Information Sciences > Supercomputer Education & Research Centre
Division of Information Sciences > BioInformatics Centre
Date Deposited: 24 Oct 2005
Last Modified: 19 Sep 2010 04:20
URI: http://eprints.iisc.ernet.in/id/eprint/3886

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