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5HDL

Crystal structure of shaft pilin spaA from Lactobacillus rhamnosus GG - E269A mutant

5HDL の概要
エントリーDOI10.2210/pdb5hdl/pdb
関連するPDBエントリー5F44 5FAA 5FGR 5FGS 5FIE 5HBB 5HTS 5J4M
分子名称Cell surface protein SpaA (2 entities in total)
機能のキーワードpilin, spaa, probiotic, isopeptide, spacba pili, adhesin, cell adhesion
由来する生物種Lactobacillus rhamnosus GG
タンパク質・核酸の鎖数3
化学式量合計91996.39
構造登録者
Chaurasia, P.,Pratap, S.,von Ossowski, I.,Palva, A.,Krishnan, V. (登録日: 2016-01-05, 公開日: 2016-07-20, 最終更新日: 2024-10-30)
主引用文献Chaurasia, P.,Pratap, S.,von Ossowski, I.,Palva, A.,Krishnan, V.
New insights about pilus formation in gut-adapted Lactobacillus rhamnosus GG from the crystal structure of the SpaA backbone-pilin subunit
Sci Rep, 6:28664-28664, 2016
Cited by
PubMed Abstract: Thus far, all solved structures of pilin-proteins comprising sortase-assembled pili are from pathogenic genera and species. Here, we present the first crystal structure of a pilin subunit (SpaA) from a non-pathogen host (Lactobacillus rhamnosus GG). SpaA consists of two tandem CnaB-type domains, each with an isopeptide bond and E-box motif. Intriguingly, while the isopeptide bond in the N-terminal domain forms between lysine and asparagine, the one in the C-terminal domain atypically involves aspartate. We also solved crystal structures of mutant proteins where residues implicated in forming isopeptide bonds were replaced. Expectedly, the E-box-substituted E139A mutant lacks an isopeptide bond in the N-terminal domain. However, the C-terminal E269A substitution gave two structures; one of both domains with their isopeptide bonds present, and another of only the N-terminal domain, but with an unformed isopeptide bond and significant conformational changes. This latter crystal structure has never been observed for any other Gram-positive pilin. Notably, the C-terminal isopeptide bond still forms in D295N-substituted SpaA, irrespective of E269 being present or absent. Although E-box mutations affect SpaA proteolytic and thermal stability, a cumulative effect perturbing normal pilus polymerization was unobserved. A model showing the polymerized arrangement of SpaA within the SpaCBA pilus is proposed.
PubMed: 27349405
DOI: 10.1038/srep28664
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 5hdl
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2025-07-09に公開中

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