5YXG

Crystal structure of C-terminal fragment of SpaD from Lactobacillus rhamnosus GG generated by limited proteolysis

Summary for 5YXG

• Entry DOI: 10.2210/pdb5yxg/pdb
• Related: 5YU5
• Descriptor: Pilus assembly protein, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: pilin, spad, probiotic, isopeptide, spafed pili, adhesin, cell adhesion
• Biological source: Lactobacillus rhamnosus GG; More
• Total number of polymer chains: 2
• Total formula weight: 69993.92

Authors

Chaurasia, P.,Pratap, S.,Palva, A.,von Ossowski, I.,Krishnan, V. (deposition date: 2017-12-05, release date: 2018-06-20, Last modification date: 2023-11-22)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.48 Å)