1b4w: Difference between revisions
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Revision as of 15:48, 30 October 2007
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BASIC PHOSPHOLIPASE A2 FROM AGKISTRODON HALYS PALLAS-IMPLICATIONS FOR ITS ASSOCIATION AND ANTICOAGULANT ACTIVITIES BY X-RAY CRYSTALLOGRAPHY
OverviewOverview
The basic phospholipase A2 (PLA2) from the venom of Agkistrodon halys, Pallas is a potent hemolytic toxin and anticoagulant. Crystal structure of, the enzyme complexed with detergent n-octyl beta-D-glucopyranoside, (beta-OG) in monoclinic crystal form has been determined to 2.6 A, resolution. Beta-OG molecules were found in the hydrophobic channels of, the enzyme. SDS-PAGE and dynamic light scattering measurements showed that, the enzyme had a strong tendency to dimerise in aqueous solution. In the, crystal structure the enzyme molecules associate into a tetramer with, pseudo 222 symmetry, and the interfacial recognition site linked dimers, constituting the tetramer have intensive interface interactions, and may, be stable in solution. The structure reveals a unique positively charged, ... [(full description)]
About this StructureAbout this Structure
1B4W is a [Single protein] structure of sequence from [Gloydius halys] with BOG as [ligand]. Active as [Phospholipase A(2)], with EC number [3.1.1.4]. Structure known Active Sites: AC1, AC2, AC3 and AC4. Full crystallographic information is available from [OCA].
ReferenceReference
Structure of basic phospholipase A2 from Agkistrodon halys Pallas: implications for its association, hemolytic and anticoagulant activities., Zhao K, Zhou Y, Lin Z, Toxicon. 2000 Jul;38(7):901-16. PMID:10728829
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