PDBsum entry 1es6

Viral protein

PDB id: 1es6

Contents

Protein chain

260 a.a.

Waters ×120

PDB id:

1es6

Name:

Viral protein

Title:

Crystal structure of the matrix protein of ebola virus

Structure:

Matrix protein vp40. Chain: a. Engineered: yes. Mutation: yes

Source:

Ebola virus sp.. Organism_taxid: 205488. Strain: zaire. Expressed in: escherichia coli. Expression_system_taxid: 562. Other_details: ebola virus RNA genome

Biol. unit:

Dimer (from PQS)

Resolution:

2.00Å R-factor: 0.220 R-free: 0.250

Authors:

A.Dessen,V.Volchkov,O.Dolnik,H.-D.Klenk,W.Weissenhorn

Key ref:

A.Dessen et al. (2000). Crystal structure of the matrix protein VP40 from Ebola virus. EMBO J, 19, 4228-4236. PubMed id: 10944105 DOI: 10.1093/emboj/19.16.4228

Date:

07-Apr-00 Release date: 30-Aug-00

Protein chain

Q77DJ6  (VP40_EBOZ5) -  Matrix protein VP40 from Zaire ebolavirus (strain Kikwit-95)

Seq: 326 a.a.

Struc: 260 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1093/emboj/19.16.4228

EMBO J 19:4228-4236 (2000)

PubMed id: 10944105

Crystal structure of the matrix protein VP40 from Ebola virus.

A.Dessen, V.Volchkov, O.Dolnik, H.D.Klenk, W.Weissenhorn.

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.

Selected figure(s)

Figure 1.
Figure 1 Stereo view of the experimental map generated with MAD phases obtained from six selenium sites identified by SOLVE and subsequently solvent flattened. The map is contoured at the 1 level, and focuses on a conserved loop region in domain 2 connecting -strands 7 and 8.

Figure 4.
Figure 4 Interdomain interactions. (A) Close up of polar interactions between the N- and C-terminal domains. Residues involved in salt bridges and hydrogen bonds are shown. For clarity, the connection between residue 307 and 310 is shown as a grey dashed line. The loop connecting both domains is indicated with an arrow. (B) Surface representation of the N-terminal domain (residues 44–194) and (C) of the C-terminal domain (residues 201–321). Hydrophobic residues lining the interface on the N- and C-terminal domains are shown in green.

The above figures are reprinted from an Open Access publication published by Macmillan Publishers Ltd: EMBO J (2000, 19, 4228-4236) copyright 2000.

Figures were selected by an automated process.