5YU5

Crystal structure of shaft pilin spaD from Lactobacillus rhamnosus GG

5YU5 の概要

• エントリーDOI: 10.2210/pdb5yu5/pdb
• 分子名称: Pilus assembly protein (2 entities in total)
• 機能のキーワード: pilin, spad, probiotic, isopeptide, spafed pili, adhesin, cell adhesion
• 由来する生物種: Lactobacillus rhamnosus GG
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 102081.46

構造登録者

Chaurasia, P.,Pratap, S.,Palva, A.,von Ossowski, I.,Krishnan, V. (登録日: 2017-11-20, 公開日: 2018-06-20, 最終更新日: 2024-10-30)

主引用文献

Chaurasia, P.,Pratap, S.,Palva, A.,von Ossowski, I.,Krishnan, V.
Bent conformation of a backbone pilin N-terminal domain supports a three-stage pilus assembly mechanism.
Commun Biol, 1:94-94, 2018

PubMed Abstract: Effective colonization of host cells by some Gram-positive bacteria often involves using lengthy, adhesive macromolecular structures called sortase-dependent pili. Among commensals, the gut-adapted GG strain encodes the operons for two varieties of these pili (SpaCBA and SpaFED), with each structure consisting of backbone, tip, and basal pilin subunits. Although the tertiary structure was recently solved for the backbone subunit (SpaA) of the SpaCBA pilus, no structural information exists for its counterpart in the SpaFED pilus. Here, we report several crystal structures for the SpaD backbone pilin, two of which capture the N-terminal domain in either the closed (linear) or open (bent) conformation. To our knowledge, this is the first observation of the bent conformation in Gram-positive pilin structures. Based on this bent conformation, we suggest a three-stage model, which we call the expose-ligate-seal mechanism, for the docking and assembly of backbone pilins into the sortase-dependent pilus.

PubMed: 30271975
DOI: 10.1038/s42003-018-0100-0

実験手法

X-RAY DIFFRACTION (2.27 Å)