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2Y1V

Full length structure of RrgB Pilus protein from Streptococcus pneumoniae

2Y1V の概要
エントリーDOI10.2210/pdb2y1v/pdb
関連するPDBエントリー2X9W 2X9X 2X9Y 2X9Z
分子名称CELL WALL SURFACE ANCHOR FAMILY PROTEIN, NICKEL (II) ION (3 entities in total)
機能のキーワードstructural protein, major pilin, pilus assembly
由来する生物種STREPTOCOCCUS PNEUMONIAE
タンパク質・核酸の鎖数3
化学式量合計196604.25
構造登録者
El-Mortaji, L.,Contreras-Martel, C.,Manzano, C.,Vernet, T.,Dessen, A.,DiGuilmi, A.M. (登録日: 2010-12-10, 公開日: 2011-11-09, 最終更新日: 2024-10-16)
主引用文献El Mortaji, L.,Contreras-Martel, C.,Moschioni, M.,Ferlenghi, I.,Manzano, C.,Vernet, T.,Dessen, A.,Di Guilmi, A.M.
The Full-Length Streptococcus Pneumoniae Major Pilin Rrgb Crystallizes in a Fibre-Like Structure, which Presents the D1 Isopeptide Bond and Provides Details on the Mechanism of Pilus Polymerization.
Biochem.J., 441:833-, 2012
Cited by
PubMed Abstract: RrgB is the major pilin which forms the pneumococcal pilus backbone. We report the high-resolution crystal structure of the full-length form of RrgB containing the IPQTG sorting motif. The RrgB fold is organized into four distinct domains, D1-D4, each of which is stabilized by an isopeptide bond. Crystal packing revealed a head-to-tail organization involving the interaction of the IPQTG motif into the D1 domain of two successive RrgB monomers. This fibrillar assembly, which fits into the electron microscopy density map of the native pilus, probably induces the formation of the D1 isopeptide bond as observed for the first time in the present study, since neither in published structures nor in soluble RrgB produced in Escherichia coli or in Streptococcus pneumoniae is the D1 bond present. Experiments performed in live bacteria confirmed that the intermolecular bond linking the RrgB subunits takes place between the IPQTG motif of one RrgB subunit and the Lys183 pilin motif residue of an adjacent RrgB subunit. In addition, we present data indicating that the D1 isopeptide bond is involved in RrgB stabilization. In conclusion, the crystal RrgB fibre is a compelling model for deciphering the molecular details required to generate the pneumococcal pilus.
PubMed: 22013894
DOI: 10.1042/BJ20111397
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.39 Å)
構造検証レポート
Validation report summary of 2y1v
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-06-18に公開中

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