1O8V

The crystal structure of Echinococcus granulosus fatty-acid-binding protein 1

1O8V の概要

• エントリーDOI: 10.2210/pdb1o8v/pdb
• 分子名称: FATTY ACID BINDING PROTEIN HOMOLOG, PALMITIC ACID (3 entities in total)
• 機能のキーワード: lipid binding protein, fatty-acid-binding protein, echinococcus granulosus, hydatid disease, fatty-acid transport
• 由来する生物種: ECHINOCOCCUS GRANULOSUS
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15387.91

構造登録者

Jakobsson, E.,Alvite, G.,Bergfors, T.,Esteves, A.,Kleywegt, G.J. (登録日: 2002-12-04, 公開日: 2003-06-19, 最終更新日: 2024-11-13)

主引用文献

Jakobsson, E.,Alvite, G.,Bergfors, T.,Esteves, A.,Kleywegt, G.J.
The Crystal Structure of Echinococcus Granulosus Fatty-Acid-Binding Protein 1
Biochim.Biophys.Acta, 1649:40-, 2003

PubMed Abstract: 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.

PubMed: 12818189
DOI: 10.1016/S1570-9639(03)00151-1

実験手法

X-RAY DIFFRACTION (1.6 Å)