1mkt Citations

1.72 A resolution refinement of the trigonal form of bovine pancreatic phospholipase A2.

Acta Crystallogr D Biol Crystallogr 54 342-6 (1998)
Cited: 6 times
EuropePMC logo PMID: 9761901

Abstract

The trigonal crystal structure of the recombinant bovine pancreatic phospholipase A2 has been re-refined at a slightly higher resolution (1.72 A). The crystals are trigonal, space group P3121, unit-cell parameters a = b = 46.78 and c = 102.89 A and are isomorphous to the previous structure. The structure was refined to a final crystallographic R value of 19.5% (Rfree = 28.4%) using 10 531 reflections. A total of 106 solvent molecules were included in the refinement compared with the earlier refinement which contains only 85 water molecules and 8 925 reflections at 1.8 A resolution. The root-mean-square deviation from the ideal bond lengths and bond angles is considerably better in the present refinement. The active site is extended ( approximately 14 A) from Ala1 to the calcium. The three catalytic residues (Asp99, His48 and the catalytic water) are connected by the conserved structural water and the N-terminal Ala1 on one side, and by the calcium through an equatorial water on the other. The water molecules play a role in the activity of the enzyme PLA2. The Ala1 end of the extended active site performs the activation of the phospholid membranes while the opposite end performs the hydrolysis of the monomeric phospholids.

Articles - 1mkt mentioned but not cited (3)

  1. 3dSS: 3D structural superposition. Sumathi K, Ananthalakshmi P, Roshan MN, Sekar K. Nucleic Acids Res 34 W128-32 (2006)
  2. Peptide-plane flipping in proteins. Hayward S. Protein Sci 10 2219-2227 (2001)
  3. Possible roles of S···O and S···N interactions in the functions and evolution of phospholipase A2. Iwaoka M, Isozumi N. Biophysics (Nagoya-shi) 2 23-34 (2006)


Articles citing this publication (3)

  1. Crystal structures of the free and anisic acid bound triple mutant of phospholipase A2. Sekar K, Vaijayanthi Mala S, Yogavel M, Velmurugan D, Poi MJ, Vishwanath BS, Gowda TV, Jeyaprakash AA, Tsai MD. J Mol Biol 333 367-376 (2003)
  2. Observation of additional calcium ion in the crystal structure of the triple mutant K56,120,121M of bovine pancreatic phospholipase A2. Rajakannan V, Yogavel M, Poi MJ, Jeyaprakash AA, Jeyakanthan J, Velmurugan D, Tsai MD, Sekar K. J Mol Biol 324 755-762 (2002)
  3. Functional Annotation from Structural Homology. Segelke BW. Methods Mol Biol 2349 215-257 (2022)


Related citations provided by authors (4)

  1. Crystal Structure of the Complex of Bovine Pancreatic Phospholipase A2 with a Transition State Analogue. Sekar K, Kumar A, Liu X, Tsai M-D, Gelb MH, Sundaralingam M To be published -
  2. Phospholipase A2 Engineering. Structural and Functional Roles of the Highly Conserved Active Site Residue Aspartate-99. Sekar K, Yu BZ, Rogers J, Lutton J, Liu X, Chen X, Tsai MD, Jain MK, Sundaralingam M Biochemistry 36 3104- (1997)
  3. Phospholipase A2 Engineering. Deletion of the C-Terminus Segment Changes Substrate Specificity and Uncouples Calcium and Substrate Binding at the Zwitterionic Interface. Huang B, Yu BZ, Rogers J, Byeon IJ, Sekar K, Chen X, Sundaralingam M, Tsai MD, Jain MK Biochemistry 35 12164- (1996)
  4. Phospholipase A2 Engineering. X-Ray Structural and Functional Evidence for the Interaction of Lysine-56 with Substrates. Noel JP, Bingman CA, Deng TL, Dupureur CM, Hamilton KJ, Jiang RT, Kwak JG, Sekharudu C, Sundaralingam M, Tsai MD Biochemistry 30 11801- (1991)