8TV0

XptA2 wild type

This is a non-PDB format compatible entry.

Summary for 8TV0

• Entry DOI: 10.2210/pdb8tv0/pdb
• Descriptor: XptA2 (1 entity in total)
• Functional Keywords: tca, insecticide, translocase, toxin
• Biological source: Xenorhabdus nematophila
• Total number of polymer chains: 5
• Total formula weight: 1435321.88

Authors

Martin, C.L.,Aller, S.G. (deposition date: 2023-08-17, release date: 2023-09-27, Last modification date: 2024-10-16)

Primary citation

Martin, C.L.,Chester, D.W.,Radka, C.D.,Pan, L.,Yang, Z.,Hart, R.C.,Binshtein, E.M.,Wang, Z.,Nagy, L.,DeLucas, L.J.,Aller, S.G.
Structures of the Insecticidal Toxin Complex Subunit XptA2 Highlight Roles for Flexible Domains.
Int J Mol Sci, 24:-, 2023

PubMed 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 from the intestine of entomopathogenic nematodes, we determined structures by X-ray crystallography and cryo-EM. Contrary to a previous report, XptA2 is pentameric. RBD-B exhibits an indentation from crystal packing that indicates loose association with the shell and a hotspot for possible receptor binding or a trigger for conformational dynamics. A two-fragment XptA2 lacking an intact linker achieved the folded pre-pore state like wild type (wt), revealing no requirement of the linker for protein folding. The linker is disordered in all structures, and we propose it plays a role in dynamics downstream of the initial pre-pore state.

PubMed: 37686027
DOI: 10.3390/ijms241713221

Experimental method

X-RAY DIFFRACTION (3.1 Å)