3ECQ

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

3ECQ の概要

• エントリーDOI: 10.2210/pdb3ecq/pdb
• 分子名称: Endo-alpha-N-acetylgalactosaminidase, CALCIUM ION, SODIUM ION, ... (5 entities in total)
• 機能のキーワード: distorted (beta/alpha)8 (tim) barrel glycoside hydrolase domain, cell wall, peptidoglycan-anchor, secreted, hydrolase
• 由来する生物種: Streptococcus pneumoniae
• 細胞内の位置: Secreted, cell wall; Peptidoglycan-anchor (By similarity): Q8DR60
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 343609.32

構造登録者

Caines, M.E.C.,Zhu, H.,Vuckovic, M.,Strynadka, N.C.J. (登録日: 2008-09-01, 公開日: 2008-09-09, 最終更新日: 2024-10-30)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.9 Å)