8tv0

XptA2 wild type

spinqualitylabelsall models 8tv0, resolution 3.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8tv0 is a 5 chain structure with sequence from Xenorhabdus nematophila. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.1Å Ligands: MSE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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 X. nematophilus 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. Structures of the Insecticidal Toxin Complex Subunit XptA2 Highlight Roles for Flexible Domains.,Martin CL, Chester DW, Radka CD, Pan L, Yang Z, Hart RC, Binshtein EM, Wang Z, Nagy L, DeLucas LJ, Aller SG Int J Mol Sci. 2023 Aug 25;24(17):13221. doi: 10.3390/ijms241713221. PMID:37686027 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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