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8TQE

XptA2 wild type

This is a non-PDB format compatible entry.
Summary for 8TQE
Entry DOI10.2210/pdb8tqe/pdb
EMDB information41503
DescriptorXptA2 (1 entity in total)
Functional Keywordstca, insecticide, translocase, toxin
Biological sourceXenorhabdus nematophila
Total number of polymer chains5
Total formula weight1421960.94
Authors
Martin, C.L.,Binshtein, E.M.,Aller, S.G. (deposition date: 2023-08-07, release date: 2023-09-27, Last modification date: 2023-10-11)
Primary citationMartin, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.1 Å)
Structure validation

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