期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 283, 期 46, 页码 31279-31283出版社
ELSEVIER
DOI: 10.1074/jbc.C800150200
关键词
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资金
- Howard Hughes Medical Institute
- Canadian Institutes of Health Research
- Michael Smith Foundation for Health Research
- Canada Foundation for Innovation
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.
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