6FQ4

Structure of Chlamydial virulence factor TarP and vinculin head domain

Summary for 6FQ4

• Entry DOI: 10.2210/pdb6fq4/pdb
• Descriptor: Vinculin, TarP-VBS1 (3 entities in total)
• Functional Keywords: translocated actin recruitment protein, vinculin-binding site, virulence factor, protein complex, cell adhesion
• Biological source: Gallus gallus (Chicken); More
• Total number of polymer chains: 2
• Total formula weight: 33510.72

Authors

Whitewood, A.J.,Singh, A.K.,Brown, D.G.,Goult, B.T. (deposition date: 2018-02-13, release date: 2018-05-09, Last modification date: 2024-01-17)

Primary citation

Whitewood, A.J.,Singh, A.K.,Brown, D.G.,Goult, B.T.
Chlamydial virulence factor TarP mimics talin to disrupt the talin-vinculin complex.
FEBS Lett., 592:1751-1760, 2018

PubMed Abstract: Vinculin is a central component of mechanosensitive adhesive complexes that form between cells and the extracellular matrix. A myriad of infectious agents mimic vinculin binding sites (VBS), enabling them to hijack the adhesion machinery and facilitate cellular entry. Here, we report the structural and biochemical characterisation of VBS from the chlamydial virulence factor TarP. Whilst the affinities of isolated VBS peptides from TarP and talin for vinculin are similar, their behaviour in larger fragments is markedly different. In talin, VBS are cryptic and require mechanical activation to bind vinculin, whereas the TarP VBS are located in disordered regions, and so are constitutively active. We demonstrate that the TarP VBS can uncouple talin:vinculin complexes, which may lead to adhesion destabilisation.

PubMed: 29710402
DOI: 10.1002/1873-3468.13074

Experimental method

X-RAY DIFFRACTION (2.89 Å)