PDBsum entry 4zgh

Sugar binding protein, toxin

PDB id: 4zgh

Contents

Protein chain

473 a.a.

Ligands

EDO ×5

PEG ×2

AUC ×2

Waters ×29

PDB id:

4zgh

Name:

Sugar binding protein, toxin

Title:

Structure of sugar binding protein pneumolysin

Structure:

Pneumolysin. Chain: a. Fragment: unp residues 2-470. Synonym: thiol-activated cytolysin. Engineered: yes. Mutation: yes

Source:

Streptococcus pneumoniae. Organism_taxid: 373153. Strain: d39 / nctc 7466. Gene: ply, spd_1726. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

Resolution:

2.90Å R-factor: 0.205 R-free: 0.307

Authors:

M.W.Parker,S.C.Feil,C.Morton

Key ref:

S.L.Lawrence et al. (2015). Crystal structure of Streptococcus pneumoniae pneumolysin provides key insights into early steps of pore formation. Sci Rep, 5, 14352. PubMed id: 26403197

Date:

23-Apr-15 Release date: 09-Mar-16

Protein chain

Q04IN8  (TACY_STRP2) -  Pneumolysin from Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466)

Seq: 471 a.a.

Struc: 473 a.a.*

* PDB and UniProt seqs differ at 4 residue positions (black crosses)

Sci Rep 5:14352 (2015)

PubMed id: 26403197

Crystal structure of Streptococcus pneumoniae pneumolysin provides key insights into early steps of pore formation.

S.L.Lawrence, S.C.Feil, C.J.Morton, A.J.Farrand, T.D.Mulhern, M.A.Gorman, K.R.Wade, R.K.Tweten, M.W.Parker.

ABSTRACT

Pore-forming proteins are weapons often used by bacterial pathogens to breach the membrane barrier of target cells. Despite their critical role in infection important structural aspects of the mechanism of how these proteins assemble into pores remain unknown. Streptococcus pneumoniae is the world's leading cause of pneumonia, meningitis, bacteremia and otitis media. Pneumolysin (PLY) is a major virulence factor of S. pneumoniae and a target for both small molecule drug development and vaccines. PLY is a member of the cholesterol-dependent cytolysins (CDCs), a family of pore-forming toxins that form gigantic pores in cell membranes. Here we present the structure of PLY determined by X-ray crystallography and, in solution, by small-angle X-ray scattering. The crystal structure reveals PLY assembles as a linear oligomer that provides key structural insights into the poorly understood early monomer-monomer interactions of CDCs at the membrane surface.