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2X9Y

STRUCTURE OF THE PILUS BACKBONE (RRGB) FROM STREPTOCOCCUS PNEUMONIAE

2X9Y の概要
エントリーDOI10.2210/pdb2x9y/pdb
関連するPDBエントリー2X9W 2X9X 2X9Z
分子名称CELL WALL SURFACE ANCHOR FAMILY PROTEIN (2 entities in total)
機能のキーワード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48163.19
構造登録者
主引用文献Spraggon, G.,Koesema, E.,Scarselli, M.,Malito, E.,Biagini, M.,Norais, N.,Emolo, C.,Barocchi, M.A.,Giusti, F.,Hilleringmann, M.,Rappuoli, R.,Lesley, S.,Covacci, A.,Masignani, V.,Ferlenghi, I.
Supramolecular Organization of the Repetitive Backbone Unit of the Streptococcus Pneumoniae Pilus.
Plos One, 5:919-, 2010
Cited by
PubMed Abstract: Streptococcus pneumoniae, like many other Gram-positive bacteria, assembles long filamentous pili on their surface through which they adhere to host cells. Pneumococcal pili are formed by a backbone, consisting of the repetition of the major component RrgB, and two accessory proteins (RrgA and RrgC). Here we reconstruct by transmission electron microscopy and single particle image reconstruction method the three dimensional arrangement of two neighbouring RrgB molecules, which represent the minimal repetitive structural domain of the native pilus. The crystal structure of the D2-D4 domains of RrgB was solved at 1.6 A resolution. Rigid-body fitting of the X-ray coordinates into the electron density map enabled us to define the arrangement of the backbone subunits into the S. pneumoniae native pilus. The quantitative fitting provide evidence that the pneumococcal pilus consists uniquely of RrgB monomers assembled in a head-to-tail organization. The presence of short intra-subunit linker regions connecting neighbouring domains provides the molecular basis for the intrinsic pilus flexibility.
PubMed: 20559564
DOI: 10.1371/JOURNAL.PONE.0010919
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.33 Å)
構造検証レポート
Validation report summary of 2x9y
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2024-10-30に公開中

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