1o8v

From Proteopedia

Revision as of 13:41, 30 October 2007

THE CRYSTAL STRUCTURE OF ECHINOCOCCUS GRANULOSUS FATTY-ACID-BINDING PROTEIN 1

Overview

We describe the 1.6 A crystal structure of the fatty-acid-binding protein, EgFABP1 from the parasitic platyhelminth Echinococcus granulosus. E., granulosus causes hydatid disease, which is a major zoonosis. EgFABP1 has, been implicated in the acquisition, storage, and transport of lipids, and, may be important to the organism since it is incapable of synthesising, most of its lipids de novo. Moreover, EgFABP1 is a promising candidate for, a vaccine against hydatid disease.The crystal structure reveals that, EgFABP1 has the expected 10-stranded beta-barrel fold typical of the, family of intracellular lipid-binding proteins, and that it is, structurally most similar to P2 myelin protein. We describe the comparison, of the crystal structure of EgFABP1 with these proteins and with an older, ... [(full description)]

About this Structure

1O8V is a [Single protein] structure of sequence from [Echinococcus granulosus] with ACE and PLM as [ligands]. Structure known Active Site: AC2. Full crystallographic information is available from [OCA].

Reference

The crystal structure of Echinococcus granulosus fatty-acid-binding protein 1., Jakobsson E, Alvite G, Bergfors T, Esteves A, Kleywegt GJ, Biochim Biophys Acta. 2003 Jun 26;1649(1):40-50. PMID:12818189

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