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TitleStructures of the Insecticidal Toxin Complex Subunit XptA2 Highlight Roles for Flexible Domains.
Journal, issue, pagesInt J Mol Sci, Vol. 24, Issue 17, Year 2023
Publish dateAug 25, 2023
AuthorsCole 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 /
PubMed AbstractThe Toxin Complex (Tc) superfamily consists of toxin translocases that contribute to the targeting, delivery, and cytotoxicity of certain pathogenic Gram-negative bacteria. Membrane receptor ...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.
External linksInt J Mol Sci / PubMed:37686027 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution3.1 Å
Structure data

41503

8tqe

EMDB-41503, PDB-8tqe:
XptA2 wild type
Method: EM (single particle) / Resolution: 3.1 Å

PDB-8tv0:
XptA2 wild type
Method: X-RAY DIFFRACTION / Resolution: 3.1 Å

Source
  • xenorhabdus nematophila (bacteria)
KeywordsTOXIN / TcA / Insecticide / Translocase

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