5HDL
Crystal structure of shaft pilin spaA from Lactobacillus rhamnosus GG - E269A mutant
5HDL の概要
エントリーDOI | 10.2210/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: 27349405DOI: 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) |
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