1faz

From Proteopedia

Revision as of 21:27, 24 November 2007

THE CRYSTAL STRUCTURE OF PROKARYOTIC PHOSPHOLIPASE A2

Overview

In this study, the x-ray crystal structures of the calcium-free and, calcium-bound forms of phospholipase A(2) (PLA(2)), produced, extracellularly by Streptomyces violaceoruber, were determined by using, the multiple isomorphous replacement and molecular replacement methods, respectively. The former and latter structures were refined to an R-factor, of 18.8% at a 1.4-A resolution and an R-factor of 15.0% at a 1.6-A, resolution, respectively. The overall structure of the prokaryotic PLA(2), exhibits a novel folding topology that demonstrates that it is completely, distinct from those of eukaryotic PLA(2)s, which have been already, determined by x-ray and NMR analyses. Furthermore, the coordination, geometry of the calcium(II) ion apparently deviated from that of, eukaryotic PLA(2)s. Regardless of the evolutionary divergence, the, catalytic mechanism including the calcium(II) ion on secreted PLA(2) seems, to be conserved between prokaryotic and eukaryotic cells. Demonstrating, that the overall structure determined by x-ray analysis is almost the same, as that determined by NMR analysis is useful to discuss the catalytic, mechanism at the molecular level of the bacterial PLA(2).

About this Structure

1FAZ is a Single protein structure of sequence from Streptomyces violaceoruber. Active as Phospholipase A(2), with EC number 3.1.1.4 Full crystallographic information is available from OCA.

Reference

The crystal structure of prokaryotic phospholipase A2., Matoba Y, Katsube Y, Sugiyama M, J Biol Chem. 2002 May 31;277(22):20059-69. Epub 2002 Mar 15. PMID:11897785

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