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The EMBO journal
Aug 15, 2000;19 (16): 4228-36.

Crystal structure of the matrix protein VP40 from Ebola virus.

A Dessen, V Volchkov, O Dolnik, H D Klenk, W Weissenhorn
Author Information
  1. A Dessen: European Molecular Biology Laboratory Grenoble Outstation, 6 rue Jules Horowitz, 38000 Grenoble, France.
PMID: 10944105 DOI: 10.1093/emboj/19.16.4228

Abstract

Ebola virus maturation occurs at the plasma membrane of infected cells and involves the clustering of the viral matrix protein VP40 at the assembly site as well as its interaction with the lipid bilayer. Here we report the X-ray crystal structure of VP40 from Ebola virus at 2.0 A resolution. The crystal structure reveals that Ebola virus VP40 is topologically distinct from all other known viral matrix proteins, consisting of two domains with unique folds, connected by a flexible linker. The C-terminal domain, which is absolutely required for membrane binding, contains large hydrophobic patches that may be involved in the interaction with lipid bilayers. Likewise, a highly basic region is shared between the two domains. The crystal structure reveals how the molecule may be able to switch from a monomeric conformation to a hexameric form, as observed in vitro. Its implications for the assembly process are discussed.

Associated Data

PDB | 1ES6

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MeSH Term

Amino Acid Sequence
Binding Sites
Cell Membrane
Crystallography, X-Ray
Ebolavirus
Lipid Bilayers
Marburgvirus
Models, Molecular
Molecular Sequence Data
Protein Conformation
Protein Structure, Secondary
Protein Structure, Tertiary
Selenium
Sequence Homology, Amino Acid
Trypsin
Viral Matrix Proteins

Chemicals

Lipid Bilayers
VP40 protein, virus
Viral Matrix Proteins
Trypsin
Selenium
Journal Article Research Support, Non-U.S. Gov't
Article has an altmetric score of 17

Word Cloud

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