Structural highlights
Function
[GH101_STRR6] Is involved in the breakdown of mucin-type O-linked glycans. Specifically removes the T-antigen disaccharide (Gal-beta-1,3-GalNAc-alpha) from extracellular host glycoproteins. Is representative of a broadly important class of virulence factors.[1] [2] [3]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Streptococcus pneumoniae endo-alpha-N-acetylgalactosaminidase is a cell surface-anchored glycoside hydrolase from family GH101 involved in the breakdown of mucin type O-linked glycans. The 189-kDa mature enzyme specifically hydrolyzes the T-antigen disaccharide from extracellular host glycoproteins and is representative of a broadly important class of virulence factors that have remained structurally uncharacterized due to their large size and highly modular nature. Here we report a 2.9 angstroms resolution crystal structure that remarkably captures the multidomain architecture and characterizes a catalytic center unexpectedly resembling that of alpha-amylases. Our analysis presents a complete model of glycoprotein recognition and provides a basis for the structure-based design of novel Streptococcus vaccines and therapeutics.
The structural basis for T-antigen hydrolysis by Streptococcus pneumoniae: a target for structure-based vaccine design.,Caines ME, Zhu H, Vuckovic M, Willis LM, Withers SG, Wakarchuk WW, Strynadka NC J Biol Chem. 2008 Nov 14;283(46):31279-83. Epub 2008 Sep 10. PMID:18784084[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Caines ME, Zhu H, Vuckovic M, Willis LM, Withers SG, Wakarchuk WW, Strynadka NC. The structural basis for T-antigen hydrolysis by Streptococcus pneumoniae: a target for structure-based vaccine design. J Biol Chem. 2008 Nov 14;283(46):31279-83. Epub 2008 Sep 10. PMID:18784084 doi:http://dx.doi.org/10.1074/jbc.C800150200
- ↑ Willis LM, Zhang R, Reid A, Withers SG, Wakarchuk WW. Mechanistic investigation of the endo-alpha-N-acetylgalactosaminidase from Streptococcus pneumoniae R6. Biochemistry. 2009 Nov 3;48(43):10334-41. doi: 10.1021/bi9013825. PMID:19788271 doi:http://dx.doi.org/10.1021/bi9013825
- ↑ Umemoto J, Bhavanandan VP, Davidson EA. Purification and properties of an endo-alpha-N-acetyl-D-galactosaminidase from Diplococcus pneumoniae. J Biol Chem. 1977 Dec 10;252(23):8609-14. PMID:21877
- ↑ Caines ME, Zhu H, Vuckovic M, Willis LM, Withers SG, Wakarchuk WW, Strynadka NC. The structural basis for T-antigen hydrolysis by Streptococcus pneumoniae: a target for structure-based vaccine design. J Biol Chem. 2008 Nov 14;283(46):31279-83. Epub 2008 Sep 10. PMID:18784084 doi:http://dx.doi.org/10.1074/jbc.C800150200
