PDBsum entry 2pr0

Toxin

PDB id: 2pr0

Contents

Protein chains

94 a.a. *

Ligands

TRS ×2

Metals

_NI ×2

Waters ×209

* Residue conservation analysis

PDB id:

2pr0

Name:

Toxin

Title:

Crystal structure of sylvaticin, a new secreted protein from pythium sylvaticum

Structure:

Sylvaticin. Chain: a, b

Source:

Pythium sylvaticum. Organism_taxid: 82950. Strain: strain 37

Resolution:

1.72Å R-factor: 0.194 R-free: 0.186

Authors:

M.B.Lascombe,T.Prange,P.Retailleau

Key ref:

M.B.Lascombe et al. (2007). Structure of sylvaticin, a new alpha-elicitin-like protein from Pythium sylvaticum. Acta Crystallogr D Biol Crystallogr, 63, 1102-1108. PubMed id: 17881828 DOI: 10.1107/S0907444907043363

Date:

03-May-07 Release date: 18-Mar-08

Protein chains

D0VWX7  (D0VWX7_9STRA) -  Elicitin from Globisporangium sylvaticum

Seq: 94 a.a.

Struc: 94 a.a.

DOI no: 10.1107/S0907444907043363

Acta Crystallogr D Biol Crystallogr 63:1102-1108 (2007)

PubMed id: 17881828

Structure of sylvaticin, a new alpha-elicitin-like protein from Pythium sylvaticum.

M.B.Lascombe, P.Retailleau, M.Ponchet, B.Industri, J.P.Blein, T.Prangé.

ABSTRACT

The structure of sylvaticin, a 10 kDa major pythin protein excreted by the parasitic oomycete Pythium sylvaticum, has been determined. Although closely related to alpha-elicitins in its biological response, toxicity and overall structure, sylvaticin presents a number of structural features that make it an unusual member of the elicitin class. Elicitins possess a large hydrophobic cavity and the mechanism of the systemic acquired resistance induced in planta is known to proceed through lipid transport and complexation within this cavity. Unlike other elicitins, sylvaticin contains tryptophan residues, one of which points inwards towards the central cavity, thus limiting access to sterols. In the case of sylvaticin, the sterol-transport mechanism is likely to be of less importance compared with other members of the elicitin family and still remains to be fully characterized.

Selected figure(s)

Figure 3.
Figure 3 Two orthogonal views of ribbon diagrams of the three-dimensional structure of sylvaticin, showing the head-to-tail dimerization of sylvaticin around the two nickel cations (green spheres) in the monoclinic form (the metal-mediated dimer). The same arrangement is also observed in the triclinic crystals.

Figure 5.
Figure 5 The hydrophobic interface between two adjacent sylvaticin dimers (the hydrophobic dimer). The packing contacts between the two neighbours involve eight phenylalanine side chains (Phe9, Phe12, Phe13, Phe75 and their symmetry-related mates).

The above figures are reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2007, 63, 1102-1108) copyright 2007.

Figures were selected by the author.