Structural highlights
Publication Abstract from PubMed
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 alpha/beta 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.
A distinct sortase SrtB anchors and processes a streptococcal adhesin AbpA with a novel structural property.,Liang X, Liu B, Zhu F, Scannapieco FA, Haase EM, Matthews S, Wu H Sci Rep. 2016 Aug 5;6:30966. doi: 10.1038/srep30966. PMID:27492581[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Liang X, Liu B, Zhu F, Scannapieco FA, Haase EM, Matthews S, Wu H. A distinct sortase SrtB anchors and processes a streptococcal adhesin AbpA with a novel structural property. Sci Rep. 2016 Aug 5;6:30966. doi: 10.1038/srep30966. PMID:27492581 doi:http://dx.doi.org/10.1038/srep30966
