PDBsum entry: 2wmg

Hydrolase

PDB-id: 2wmg

Main view

Contents

Description

Header details

Header records

References

PROCHECK

Protein chain

553 a.a. *

Ligands

FUC-GAL-NAG-FUC

Waters ×334

* Residue conservation analysis

Tools

Clefts Calculation

Bottom view	Right view

PDB id:

2wmg

Name:

Hydrolase

Title:

Crystal structure of the catalytic module of a family 98 glycoside hydrolase from streptococcus pneumoniae tigr4 ( sp4gh98) in complex with the lewisy pentasaccharide blood group antigen.

Structure:

Fucolectin-related protein. Chain: a. Fragment: catalytic module, residues 31-589. Synonym: glycoside hydrolase. Engineered: yes. Mutation: yes

Source:

Streptococcus pneumoniae. Organism_taxid: 170187. Strain: tigr4. Atcc: baa-334. Expressed in: escherichia coli. Expression_system_taxid: 469008.

UniProt:

Q97N96 (Q97N96_STRPN)

Seq:

Struc:

Seq:

Struc:

Seq:

Struc:

Seq:

Struc:

Seq:

1038 a.a.

Struc:

553 a.a.*

Key:

PfamA domain

Secondary structure

* PDB and UniProt seqs differ at 2 residue positions (black crosses)

Resolution:

2.30Å

R-factor:

0.159

R-free:

0.227

Authors:

M.A.Higgins,G.E.Whitworth,N.El Warry,M.Randriantsoa, E.Samain,R.D.Burke,D.J.Vocadlo,A.B.Boraston

Key ref:

M.A.Higgins et al. (2009). Differential recognition and hydrolysis of host carbohydrate antigens by Streptococcus pneumoniae family 98 glycoside hydrolases.. J Biol Chem, 284, 26161-26173. [PubMed id: 19608744] [DOI: 10.1074/jbc.M109.024067]

Date:

30-Jun-09

Release date:

14-Jul-09

Related entries:

2j1u structure of a streptococcus pneumoniae fucose binding module in complex with the blood group a-tetrasaccharide
2j22 structure of a streptococcus pneumoniae fucose binding module, spx-3
2j1s structure of a streptococcus pneumoniae fucose binding module in complex with fucose
2j1v structure of a streptococcus pneumoniae fucose binding module in complex with the blood group h-trisaccharide
2j1t structure of a streptococcus pneumoniae fucose binding module in complex with the lewis y antigen
2j1r structure of a streptococcus pneumoniae fucose binding module
2wmf crystal structure of the catalytic module of a family 98 glycoside hydrolase from streptococcus pneumoniae tigr4 (sp4gh98) in its native form.
2wmh crystal structure of the catalytic module of a family 98 glycoside hydrolase from streptococcus pneumoniae tigr4 in complex with the h-disaccharide blood group antigen.

Quick_links

Procheck

Clefts

Surface

Key reference

DOI no: 10.1074/jbc.M109.024067

J Biol Chem 284:26161-26173 (2009)

PubMed id: 19608744

Differential recognition and hydrolysis of host carbohydrate antigens by Streptococcus pneumoniae family 98 glycoside hydrolases.

M.A.Higgins, G.E.Whitworth, N.El Warry, M.Randriantsoa, E.Samain, R.D.Burke, D.J.Vocadlo, A.B.Boraston.

ABSTRACT

The presence of a fucose utilization operon in the Streptococcus pneumoniae genome and its established importance in virulence indicates a reliance of this bacterium on the harvesting of host fucose-containing glycans. The identities of these glycans, however, and how they are harvested is presently unknown. The biochemical and high resolution x-ray crystallographic analysis of two family 98 glycoside hydrolases (GH98s) from distinctive forms of the fucose utilization operon that originate from different S. pneumoniae strains reveal that one enzyme, the predominant type among pneumococcal isolates, has a unique endo-beta-galactosidase activity on the LewisY antigen. Altered active site topography in the other species of GH98 enzyme tune its endo-beta-galactosidase activity to the blood group A and B antigens. Despite their different specificities, these enzymes, and by extension all family 98 glycoside hydrolases, use an inverting catalytic mechanism. Many bacterial and viral pathogens exploit host carbohydrate antigens for adherence as a precursor to colonization or infection. However, this is the first evidence of bacterial endoglycosidase enzymes that are known to play a role in virulence and are specific for distinct host carbohydrate antigens. The strain-specific distribution of two distinct types of GH98 enzymes further suggests that S. pneumoniae strains may specialize to exploit host-specific antigens that vary from host to host, a factor that may feature in whether a strain is capable of colonizing a host or establishing an invasive infection.