2WW8

Structure of the pilus adhesin (RrgA) from Streptococcus pneumoniae

2WW8 の概要

• エントリーDOI: 10.2210/pdb2ww8/pdb
• 分子名称: CELL WALL SURFACE ANCHOR FAMILY PROTEIN, MAGNESIUM ION, CALCIUM ION, ... (5 entities in total)
• 機能のキーワード: igg, pilus, cna_b, adhesin, integrin, cell adhesion
• 由来する生物種: STREPTOCOCCUS PNEUMONIAE
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 100426.51

構造登録者

Izore, T.,Contreras-Martel, C.,El-Mortaji, L.,Manzano, C.,Terrasse, R.,Vernet, T.,Di-Guilmi, A.M.,Dessen, A. (登録日: 2009-10-22, 公開日: 2010-01-19, 最終更新日: 2024-10-16)

主引用文献

Izore, T.,Contreras-Martel, C.,El-Mortaji, L.,Manzano, C.,Terrasse, R.,Vernet, T.,Di-Guilmi, A.M.,Dessen, A.
Structural Basis of Host Cell Recognition by the Pilus Adhesin from Streptococcus Pneumoniae
Structure, 18:106-, 2010

PubMed Abstract: Pili are fibrous virulence factors associated directly to the bacterial surface that play critical roles in adhesion and recognition of host cell receptors. The human pathogen Streptococcus pneumoniae carries a single pilus-related adhesin (RrgA) that is key for infection establishment and provides protection from bacterial challenge in animal infection models, but details of these roles remain unclear. Here we report the high-resolution crystal structure of RrgA, a 893-residue elongated macromolecule whose fold contains four domains presenting both eukaryotic and prokaryotic origins. RrgA harbors an integrin I collagen-recognition domain decorated with two inserted "arms" that fold into a positively charged cradle, as well as three "stalk-forming" domains. We show by site-specific mutagenesis, mass spectrometry, and thermal shift assays that intradomain isopeptide bonds play key roles in stabilizing RrgA's stalk. The high sequence similarity between RrgA and its homologs in other Gram-positive microorganisms suggests common strategies for ECM recognition and immune evasion.

PubMed: 20152157
DOI: 10.1016/J.STR.2009.10.019

実験手法

X-RAY DIFFRACTION (1.9 Å)