1psj
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(New page: 200px<br /><applet load="1psj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1psj, resolution 2.0Å" /> '''ACIDIC PHOSPHOLIPASE ...)
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Revision as of 21:58, 20 November 2007
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ACIDIC PHOSPHOLIPASE A2 FROM AGKISTRODON HALYS PALLAS
Overview
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.
About this Structure
1PSJ is a Single protein structure of sequence from Gloydius halys with CA as ligand. Active as Phospholipase A(2), with EC number 3.1.1.4 Full crystallographic information is available from OCA.
Reference
Crystal structure of an acidic phospholipase A2 from the venom of Agkistrodon halys pallas at 2.0 A resolution., Wang XQ, Yang J, Gui LL, Lin ZJ, Chen YC, Zhou YC, J Mol Biol. 1996 Feb 9;255(5):669-76. PMID:8636969
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