3ecq | pdb_00003ecq
Endo-alpha-N-acetylgalactosaminidase from Streptococcus pneumoniae: SeMet structure
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 PubMedStreptococcus 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
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