3B2M

Crystal Structure of the Major Pilin from Streptococcus pyogenes

3B2M の概要

• エントリーDOI: 10.2210/pdb3b2m/pdb
• 分子名称: Putative uncharacterized protein SPy0128 (2 entities in total)
• 機能のキーワード: all-beta, pili, isopeptide, cell adhesion, structural protein
• 由来する生物種: Streptococcus pyogenes serotype M1
• 細胞内の位置: Secreted, cell wall; Peptidoglycan-anchor: Q9A1S2
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 97440.01

構造登録者

Kang, H.J.,Coulibaly, F.,Proft, T.,Baker, E.N. (登録日: 2007-10-18, 公開日: 2007-12-18, 最終更新日: 2024-10-30)

主引用文献

Kang, H.J.,Coulibaly, F.,Clow, F.,Proft, T.,Baker, E.N.
Stabilizing isopeptide bonds revealed in gram-positive bacterial pilus structure.
Science, 318:1625-1628, 2007

PubMed Abstract: Many bacterial pathogens have long, slender pili through which they adhere to host cells. The crystal structure of the major pilin subunit from the Gram-positive human pathogen Streptococcus pyogenes at 2.2 angstroms resolution reveals an extended structure comprising two all-beta domains. The molecules associate in columns through the crystal, with each carboxyl terminus adjacent to a conserved lysine of the next molecule. This lysine forms the isopeptide bonds that link the subunits in native pili, validating the relevance of the crystal assembly. Each subunit contains two lysine-asparagine isopeptide bonds generated by an intramolecular reaction, and we find evidence for similar isopeptide bonds in other cell surface proteins of Gram-positive bacteria. The present structure explains the strength and stability of such Gram-positive pili and could facilitate vaccine development.

PubMed: 18063798
DOI: 10.1126/science.1145806

実験手法

X-RAY DIFFRACTION (2.22 Å)