2ND4

A distinct sortase SrtB anchors and processes a streptococcal adhesin AbpA with a novel structural property

2ND4 の概要

• エントリーDOI: 10.2210/pdb2nd4/pdb
• NMR情報: BMRB: 19866
• 分子名称: Amylase-binding protein AbpA (1 entity in total)
• 機能のキーワード: novel fold, hydrolase receptor
• 由来する生物種: Streptococcus parasanguinis FW213
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 19123.78

構造登録者

Liu, B.,Zhu, F.,Wu, H.,Matthews, S. (登録日: 2016-05-05, 公開日: 2016-09-07, 最終更新日: 2024-05-01)

主引用文献

Liang, X.,Liu, B.,Zhu, F.,Scannapieco, F.A.,Haase, E.M.,Matthews, S.,Wu, H.
A distinct sortase SrtB anchors and processes a streptococcal adhesin AbpA with a novel structural property.
Sci Rep, 6:30966-30966, 2016

PubMed Abstract: Surface display of proteins by sortases in Gram-positive bacteria is crucial for bacterial fitness and virulence. We found a unique gene locus encoding an amylase-binding adhesin AbpA and a sortase B in oral streptococci. AbpA possesses a new distinct C-terminal cell wall sorting signal. We demonstrated that this C-terminal motif is required for anchoring AbpA to cell wall. In vitro and in vivo studies revealed that SrtB has dual functions, anchoring AbpA to the cell wall and processing AbpA into a ladder profile. Solution structure of AbpA determined by NMR reveals a novel structure comprising a small globular α/β domain and an extended coiled-coil heliacal domain. Structural and biochemical studies identified key residues that are crucial for amylase binding. Taken together, our studies document a unique sortase/adhesion substrate system in streptococci adapted to the oral environment rich in salivary amylase.

PubMed: 27492581
DOI: 10.1038/srep30966

実験手法

SOLUTION NMR