1PSJ

ACIDIC PHOSPHOLIPASE A2 FROM AGKISTRODON HALYS PALLAS

Summary for 1PSJ

• Entry DOI: 10.2210/pdb1psj/pdb
• Descriptor: PHOSPHOLIPASE A2, CALCIUM ION (3 entities in total)
• Functional Keywords: hydrolase, lipid degradation, calcium
• Biological source: Gloydius halys (halys viper)
• Cellular location: Secreted: P14418
• Total number of polymer chains: 1
• Total formula weight: 14028.89

Authors

Wang, X.Q.,Lin, Z.J. (deposition date: 1995-05-24, release date: 1996-07-11, Last modification date: 2024-11-06)

Primary citation

Wang, X.Q.,Yang, J.,Gui, L.L.,Lin, Z.J.,Chen, Y.C.,Zhou, Y.C.
Crystal structure of an acidic phospholipase A2 from the venom of Agkistrodon halys pallas at 2.0 A resolution.
J.Mol.Biol., 255:669-676, 1996

PubMed Abstract: The crystal structure of acidic phospholipase A2 from the venom of Agkistrodon halys pallas has been determined by molecular replacement at 2.0 A resolution to a crystallographic R-factor of 0.157. The overall structure of the molecule is very similar to those of other phospholipase A2 species of known structure. The catalytic site, the hydrophobic channel and the N-terminal region show greatest structural conservation. The Ca(2+)-binding region has a conformation that resembles closely that of bovine PLA2 rather than Crotalus atrox PLA2. Compared with other PLA2 species, the conformation of the C-terminal ridge shows significant difference due to the insertion of two residues. A unique aromatic patch appears on one face of the molecules, surrounded by two acidic residues, the relevant features of this structure and their possible biological implications are discussed.

PubMed: 8636969
DOI: 10.1006/jmbi.1996.0054

Experimental method

X-RAY DIFFRACTION (2 Å)