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1poa

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Revision as of 21:50, 20 November 2007 by OCA (Talk | contribs)
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1poa, resolution 1.5Å

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INTERFACIAL CATALYSIS: THE MECHANISM OF PHOSPHOLIPASE A2

Overview

A chemical description of the action of phospholipase A2 (PLA2) can now be, inferred with confidence from three high-resolution x-ray crystal, structures. The first is the structure of the PLA2 from the venom of the, Chinese cobra (Naja naja atra) in a complex with a phosphonate, transition-state analogue. This enzyme is typical of a large, well-studied, homologous family of PLA2S. The second is a similar complex with the, evolutionarily distant bee-venom PLA2. The third structure is the, uninhibited PLA2 from Chinese cobra venom. Despite the different molecular, architectures of the cobra and bee-venom PLA2s, the transition-state, analogue interacts in a nearly identical way with the catalytic machinery, of both enzymes. The disposition of the fatty-acid side chains suggests a, common access route of the substrate from its position in the lipid, aggregate to its productive interaction with the active site. Comparison, of the cobra-venom complex with the uninhibited enzyme indicates that, optimal binding and catalysis at the lipid-water interface is due to, facilitated substrate diffusion from the interfacial binding surface to, the catalytic site rather than an allosteric change in the enzyme's, structure. However, a second bound calcium ion changes its position upon, the binding of the transition-state analogue, suggesting a mechanism for, augmenting the critical electrophile.

About this Structure

1POA is a Single protein structure of sequence from Naja atra with CA as ligand. Active as Phospholipase A(2), with EC number 3.1.1.4 Full crystallographic information is available from OCA.

Reference

Interfacial catalysis: the mechanism of phospholipase A2., Scott DL, White SP, Otwinowski Z, Yuan W, Gelb MH, Sigler PB, Science. 1990 Dec 14;250(4987):1541-6. PMID:2274785

Page seeded by OCA on Tue Nov 20 23:58:07 2007

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