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.

Summary for 2WMH

• Entry DOI: 10.2210/pdb2wmh/pdb
• Related: 2J1R 2J1S 2J1T 2J1U 2J1V 2J22 2WMF 2WMG
• Descriptor: FUCOLECTIN-RELATED PROTEIN, alpha-L-fucopyranose-(1-2)-beta-D-galactopyranose (3 entities in total)
• Functional Keywords: hydrolase, glycoside hydrolase, streptococcus pneumoniae, blood group antigen, fucose utilization
• Biological source: STREPTOCOCCUS PNEUMONIAE
• Total number of polymer chains: 1
• Total formula weight: 67111.99

Authors

Higgins, M.A.,Whitworth, G.E.,El Warry, N.,Randriantsoa, M.,Samain, E.,Burke, R.D.,Vocadlo, D.J.,Boraston, A.B. (deposition date: 2009-06-30, release date: 2009-07-14, Last modification date: 2024-05-08)

Primary citation

Higgins, M.A.,Whitworth, G.E.,El Warry, N.,Randriantsoa, M.,Samain, E.,Burke, R.D.,Vocadlo, D.J.,Boraston, A.B.
Differential Recognition and Hydrolysis of Host Carbohydrate-Antigens by Streptococcus Pneumoniae Family 98 Glycoside Hydrolases.
J.Biol.Chem., 284:26161-, 2009

PubMed 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.

PubMed: 19608744
DOI: 10.1074/JBC.M109.024067

Experimental method

X-RAY DIFFRACTION (1.7 Å)