2KUB

Solution structure of the alpha subdomain of the major non-repeat unit of Fap1 fimbriae of Streptococcus parasanguis

2KUB の概要

• エントリーDOI: 10.2210/pdb2kub/pdb
• 分子名称: Fimbriae-associated protein Fap1 (1 entity in total)
• 機能のキーワード: helical bundle, cell wall, peptidoglycan-anchor, structural protein
• 由来する生物種: Streptococcus parasanguinis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 8819.99

構造登録者

Ramboarina, S.,Garnett, J.A.,Bodey, A.,Simpson, P.,Bardiaux, B.,Nilges, M.,Matthews, S. (登録日: 2010-02-17, 公開日: 2010-07-21, 最終更新日: 2024-05-29)

主引用文献

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

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: 20584910
DOI: 10.1074/jbc.M110.128165

実験手法

SOLUTION NMR