3ECQ

Endo-alpha-N-acetylgalactosaminidase from Streptococcus pneumoniae: SeMet structure

Summary for 3ECQ

• Entry DOI: 10.2210/pdb3ecq/pdb
• Descriptor: Endo-alpha-N-acetylgalactosaminidase, CALCIUM ION, SODIUM ION, ... (5 entities in total)
• Functional Keywords: distorted (beta/alpha)8 (tim) barrel glycoside hydrolase domain, cell wall, peptidoglycan-anchor, secreted, hydrolase
• Biological source: Streptococcus pneumoniae
• Cellular location: Secreted, cell wall; Peptidoglycan-anchor (By similarity): Q8DR60
• Total number of polymer chains: 2
• Total formula weight: 343609.32

Authors

Caines, M.E.C.,Zhu, H.,Vuckovic, M.,Strynadka, N.C.J. (deposition date: 2008-09-01, release date: 2008-09-09, Last modification date: 2024-10-30)

Primary citation

Caines, M.E.,Zhu, H.,Vuckovic, M.,Willis, L.M.,Withers, S.G.,Wakarchuk, W.W.,Strynadka, N.C.
The structural basis for T-antigen hydrolysis by Streptococcus pneumoniae: a target for structure-based vaccine design.
J.Biol.Chem., 283:31279-31283, 2008

PubMed 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 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.

PubMed: 18784084
DOI: 10.1074/jbc.C800150200

Experimental method

X-RAY DIFFRACTION (2.9 Å)