1VL9

Atomic resolution (0.97A) structure of the triple mutant (K53,56,121M) of bovine pancreatic phospholipase A2

Summary for 1VL9

• Entry DOI: 10.2210/pdb1vl9/pdb
• Descriptor: Phospholipase A2, CALCIUM ION, CHLORIDE ION, ... (6 entities in total)
• Functional Keywords: alpha helix, beta sheet, triple mutant, calcium ion, hydrolase
• Biological source: Bos taurus (cattle)
• Cellular location: Secreted: P00593
• Total number of polymer chains: 1
• Total formula weight: 14641.21

Authors

Sekar, K.,Velmurugan, D.,Rajakannan, V.,Gayathri, D.,Poi, M.-J.,Tsai, M.-D.,Dauter, M.,Dauter, Z. (deposition date: 2004-07-15, release date: 2004-10-19, Last modification date: 2023-12-27)

Primary citation

Sekar, K.,Rajakannan, V.,Gayathri, D.,Velmurugan, D.,Poi, M.J.,Dauter, M.,Dauter, Z.,Tsai, M.D.
Atomic resolution (0.97 A) structure of the triple mutant (K53,56,121M) of bovine pancreatic phospholipase A2.
Acta Crystallogr.,Sect.F, 61:3-7, 2005

PubMed Abstract: The enzyme phospholipase A2 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 A2 in which the lysine residues at positions 53, 56 and 121 are replaced recombinantly by methionines has been determined at atomic resolution (0.97 A). The crystal is monoclinic (space group P2), with unit-cell parameters a = 36.934, b = 23.863, c = 65.931 A, beta = 101.47 degrees. The structure was solved by molecular replacement and has been refined to a final R factor of 10.6% (Rfree = 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.

PubMed: 16508077
DOI: 10.1107/S1744309104021748

Experimental method

X-RAY DIFFRACTION (0.97 Å)