2ND4
A distinct sortase SrtB anchors and processes a streptococcal adhesin AbpA with a novel structural property
Summary for 2ND4
| Entry DOI | 10.2210/pdb2nd4/pdb |
| NMR Information | BMRB: 19866 |
| Descriptor | Amylase-binding protein AbpA (1 entity in total) |
| Functional Keywords | novel fold, hydrolase receptor |
| Biological source | Streptococcus parasanguinis FW213 |
| Total number of polymer chains | 1 |
| Total formula weight | 19123.78 |
| Authors | Liu, B.,Zhu, F.,Wu, H.,Matthews, S. (deposition date: 2016-05-05, release date: 2016-09-07, Last modification date: 2024-05-01) |
| Primary citation | 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 Cited by 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: 27492581DOI: 10.1038/srep30966 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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