1o8v
From Proteopedia
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==Overview== | ==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, ... | + | 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, homology model for EgFABP1.The electron density reveals the presence of a, bound ligand inside the cavity, which we have interpreted as palmitic, acid. The carboxylate group of the fatty acid interacts with the protein's, P2 motif, consisting of a conserved triad R em leader R-x-Y. The, hydrophobic tail of the ligand assumes a fairly flat, U-shaped, conformation and has relatively few interactions with the protein.We, discuss some of the structural implications of the crystal structure of, EgFABP1 for related platyhelminthic FABPs. |
==About this Structure== | ==About this Structure== | ||
| - | 1O8V is a | + | 1O8V is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Echinococcus_granulosus Echinococcus granulosus] with ACE and PLM as [http://en.wikipedia.org/wiki/ligands ligands]. Structure known Active Site: AC2. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1O8V OCA]. |
==Reference== | ==Reference== | ||
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[[Category: hydatid disease]] | [[Category: hydatid disease]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 14:00:05 2007'' |
Revision as of 11:54, 5 November 2007
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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, homology model for EgFABP1.The electron density reveals the presence of a, bound ligand inside the cavity, which we have interpreted as palmitic, acid. The carboxylate group of the fatty acid interacts with the protein's, P2 motif, consisting of a conserved triad R em leader R-x-Y. The, hydrophobic tail of the ligand assumes a fairly flat, U-shaped, conformation and has relatively few interactions with the protein.We, discuss some of the structural implications of the crystal structure of, EgFABP1 for related platyhelminthic FABPs.
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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