2KUB
Solution structure of the alpha subdomain of the major non-repeat unit of Fap1 fimbriae of Streptococcus parasanguis
Summary for 2KUB
| Entry DOI | 10.2210/pdb2kub/pdb |
| Descriptor | Fimbriae-associated protein Fap1 (1 entity in total) |
| Functional Keywords | helical bundle, cell wall, peptidoglycan-anchor, structural protein |
| Biological source | Streptococcus parasanguinis |
| Total number of polymer chains | 1 |
| Total formula weight | 8819.99 |
| Authors | Ramboarina, S.,Garnett, J.A.,Bodey, A.,Simpson, P.,Bardiaux, B.,Nilges, M.,Matthews, S. (deposition date: 2010-02-17, release date: 2010-07-21, Last modification date: 2024-05-29) |
| Primary citation | Ramboarina, S.,Garnett, J.A.,Zhou, M.,Li, Y.,Peng, Z.,Taylor, J.D.,Lee, W.C.,Bodey, A.,Murray, J.W.,Alguel, Y.,Bergeron, J.,Bardiaux, B.,Sawyer, E.,Isaacson, R.,Tagliaferri, C.,Cota, E.,Nilges, M.,Simpson, P.,Ruiz, T.,Wu, H.,Matthews, S. Structural insights into serine-rich fimbriae from gram-positive bacteria. J.Biol.Chem., 2010 Cited by PubMed Abstract: The serine-rich repeat family of fimbriae play important roles in the pathogenesis of streptococci and staphylococci. Despite recent attention, their finer structural details and precise adhesion mechanisms have yet to be determined. Fap1 (Fimbriae-associated protein 1) is the major structural subunit of serine-rich repeat fimbriae from Streptococcus parasanguinis and plays an essential role in fimbrial biogenesis, adhesion, and the early stages of dental plaque formation. Combining multidisciplinary, high resolution structural studies with biological assays, we provide new structural insight into adhesion by Fap1. We propose a model in which the serine-rich repeats of Fap1 subunits form an extended structure that projects the N-terminal globular domains away from the bacterial surface for adhesion to the salivary pellicle. We also uncover a novel pH-dependent conformational change that modulates adhesion and likely plays a role in survival in acidic environments. PubMed: 20584910DOI: 10.1074/jbc.M110.128165 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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