@article { ISI:000260760800003,
	title = {The Structural Basis for T-antigen Hydrolysis by Streptococcus pneumoniae A TARGET FOR STRUCTURE-BASED VACCINE DESIGN},
	journal = {JOURNAL OF BIOLOGICAL CHEMISTRY},
	volume = {283},
	number = {46},
	year = {2008},
	month = {NOV 14},
	pages = {31279-31283},
	abstract = {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 angstrom 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.},
	issn = {0021-9258},
	doi = {10.1074/jbc.C800150200},
	author = {Caines, Matthew E. C. and Zhu, Haizhong and Vuckovic, Marija and Willis, Lisa M. and Withers, Stephen G. and Wakarchuk, Warren W. and Strynadka, Natalie C. J.}
}
