4OQ1

Structure of the Streptococcal ancillary pilin

4OQ1 の概要

• エントリーDOI: 10.2210/pdb4oq1/pdb
• 分子名称: Cell wall surface anchor family protein (2 entities in total)
• 機能のキーワード: cnab domain, igg-rev fold, pilin protein, 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: 41970.11

構造登録者

Shaik, M.M.,Di Guilmi, A.M.,Dessen, A. (登録日: 2014-02-07, 公開日: 2014-04-23, 最終更新日: 2024-11-06)

主引用文献

Shaik, M.M.,Maccagni, A.,Tourcier, G.,Di Guilmi, A.M.,Dessen, A.
Structural Basis of Pilus Anchoring by the Ancillary Pilin RrgC of Streptococcus pneumoniae.
J.Biol.Chem., 289:16988-16997, 2014

PubMed Abstract: Pili are surface-attached, fibrous virulence factors that play key roles in the pathogenesis process of a number of bacterial agents. Streptococcus pneumoniae is a causative agent of pneumonia and meningitis, and the appearance of drug-resistance organisms has made its treatment challenging, especially in developing countries. Pneumococcus-expressed pili are composed of three structural proteins: RrgB, which forms the polymerized backbone, RrgA, the tip-associated adhesin, and RrgC, which presumably associates the pilus with the bacterial cell wall. Despite the fact that the structures of both RrgA and RrgB were known previously, structural information for RrgC was still lacking, impeding the analysis of a complete model of pilus architecture. Here, we report the structure of RrgC to 1.85 Å and reveal that it is a three-domain molecule stabilized by two intradomain isopeptide bonds. RrgC does not depend on pilus-specific sortases to become attached to the cell wall; instead, it binds the preformed pilus to the peptidoglycan by employing the catalytic activity of SrtA. A comprehensive model of the type 1 pilus from S. pneumoniae is also presented.

PubMed: 24755220
DOI: 10.1074/jbc.M114.555854

実験手法

X-RAY DIFFRACTION (1.85 Å)