PDBsum entry 2w3y

Lipid binding protein

PDB id: 2w3y

Contents

Protein chains

267 a.a.

Ligands

PLM ×2

Waters ×362

PDB id:

2w3y

Name:

Lipid binding protein

Title:

Structure of the evf virulence factor

Structure:

Virulence factor. Chain: a, b. Synonym: evf. Engineered: yes

Source:

Pectobacterium carotovorum subsp. Carotovorum. Organism_taxid: 555. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

2.00Å R-factor: 0.203 R-free: 0.250

Authors:

S.Quevillon-Cheruel,N.Leulliot,C.Acosta Muniz C,M.Vincent,J.Gallay, M.Argentini,D.Cornu,F.Boccard,B.Lemaitre,H.Van Tilbeurgh

Key ref:

S.Quevillon-Cheruel et al. (2009). Evf, a Virulence Factor Produced by the Drosophila Pathogen Erwinia carotovora, Is an S-Palmitoylated Protein with a New Fold That Binds to Lipid Vesicles. J Biol Chem, 284, 3552-3562. PubMed id: 18978353 DOI: 10.1074/jbc.M808334200

Date:

17-Nov-08 Release date: 30-Dec-08

Protein chains

Q8GCR2  (Q8GCR2_PECCC) -  Virulence factor from Pectobacterium carotovorum subsp. carotovorum

Seq: 277 a.a.

Struc: 267 a.a.

DOI no: 10.1074/jbc.M808334200

J Biol Chem 284:3552-3562 (2009)

PubMed id: 18978353

Evf, a Virulence Factor Produced by the Drosophila Pathogen Erwinia carotovora, Is an S-Palmitoylated Protein with a New Fold That Binds to Lipid Vesicles.

S.Quevillon-Cheruel, N.Leulliot, C.A.Muniz, M.Vincent, J.Gallay, M.Argentini, D.Cornu, F.Boccard, B.Lemaître, H.van Tilbeurgh.

ABSTRACT

Erwinia carotovora are phytopathogenic Gram-negative bacteria of agronomic interest as these bacteria are responsible for fruit soft rot and use insects as dissemination vectors. The Erwinia carotovora carotovora strain 15 (Ecc15) is capable of persisting in the Drosophila gut by the sole action of one protein, Erwinia virulence factor (Evf). However, the precise function of Evf is elusive, and its sequence does not provide any indication as to its biochemical function. We have solved the 2.0-A crystal structure of Evf and found a protein with a complex topology and a novel fold. The structure of Evf confirms that Evf is unlike any virulence factors known to date. Most remarkably, we identified palmitoic acid covalently bound to the totally conserved Cys(209), which provides important clues as to the function of Evf. Mutation of the palmitoic binding cysteine leads to a loss of virulence, proving that palmitoylation is at the heart of Evf infectivity and may be a membrane anchoring signal. Fluorescence studies of the sole tryptophan residue (Trp(94)) demonstrated that Evf was indeed able to bind to model membranes containing negatively charged phospholipids and to promote their aggregation.

Selected figure(s)

Figure 1.
Structure of Evf. A, topology diagram of Evf. Helices (circles) and strands (triangles) are colored using the same code as in B. B, schematic stereographic presentation of Evf. C, same as B rotated 90°.

Figure 8.
Evf-mediated membrane aggregation. SUV aggregation was measured by turbidimetry at 340 nm at pH 7.2 (open circles) and pH 5 (black trace). Lipid/protein ratio = 200.

The above figures are reprinted by permission from the ASBMB: J Biol Chem (2009, 284, 3552-3562) copyright 2009.

Figures were selected by an automated process.