Structures of the Insecticidal Toxin Complex Subunit XptA2 Highlight Roles for Flexible Domains

Authors

Cole L Martin
David W Chester
Christopher D Radka
Lurong Pan
Zhengrong Yang
Rachel C Hart
Elad M Binshtein
Zhao Wang
Lisa Nagy
Lawrence J DeLucas
Stephen G Aller

Publication Date

8-25-2023

Journal

International Journal of Molecular Sciences

DOI

10.3390/ijms241713221

PMID

37686027

PMCID

: PMC10487846

PubMedCentral® Posted Date

8-26-2023

PubMedCentral® Full Text Version

Post-print

Published Open-Access

yes

Keywords

Insecticides, Bandages, Biological Transport, Crystallography, X-Ray, Protein Folding, Toxins, Biological, TcA, toxin translocase, Cryo-EM, X-ray crystallography

Abstract

The Toxin Complex (Tc) superfamily consists of toxin translocases that contribute to the targeting, delivery, and cytotoxicity of certain pathogenic Gram-negative bacteria. Membrane receptor targeting is driven by the A-subunit (TcA), which comprises IgG-like receptor binding domains (RBDs) at the surface. To better understand XptA2, an insect specific TcA secreted by the symbiont