3PHS

Crystal Structure of GBS52, the minor pilin in gram-positive pathogen Streptococcus agalactiae

「2PZ4」から置き換えられました

3PHS の概要

• エントリーDOI: 10.2210/pdb3phs/pdb
• 関連するPDBエントリー: 3PF2
• 分子名称: Cell wall surface anchor family protein (2 entities in total)
• 機能のキーワード: ig-like fold, igg-rev fold, gbs52, streptococcus agalactiae, gram-positive pilins, adhesions, cell adhesion, cell wall anchoring, adhesion, pilus subunit, isopeptide bond, gram-positive bacterial cell wall, structural protein, cell ahdesion
• 由来する生物種: Streptococcus agalactiae
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 27692.24

構造登録者

Narayana, S.V.L.,Krishnan, V. (登録日: 2010-11-04, 公開日: 2010-11-17, 最終更新日: 2024-11-20)

主引用文献

Krishnan, V.,Gaspar, A.H.,Ye, N.,Mandlik, A.,Ton-That, H.,Narayana, S.V.
An IgG-like domain in the minor pilin GBS52 of Streptococcus agalactiae mediates lung epithelial cell adhesion.
Structure, 15:893-903, 2007

PubMed Abstract: Streptococcus agalactiae is the leading cause of neonatal pneumonia, sepsis, and meningitis. The pathogen assembles heterotrimeric pilus structures on its surface; however, their function in pathogenesis is poorly understood. We report here the crystal structure of the pilin GBS52, which reveals two IgG-like fold domains, N1 and N2. Each domain is comprised of seven antiparallel beta strands, an arrangement similar to the fold observed in the Staphylococcus aureus adhesin Cna. Consistent with its role as an adhesin, deletion of gbs52 gene significantly reduces bacterial adherence to pulmonary epithelial cells. Moreover, latex beads linked to the GBS52 protein adhere to pulmonary but not to many other epithelial cells; binding to the former is specifically inhibited by antibodies against GBS52. Nonetheless, substantial binding is only observed with N2 domain-conjugated beads. This study presents the structure of a Gram-positive pilin that utilizes a distinct IgG fold variant to mediate pathogen adherence to a specific tissue.

PubMed: 17697995
DOI: 10.1016/j.str.2007.06.015

実験手法

X-RAY DIFFRACTION (1.8 Å)