6BL9

NMR Solution structure of U-SLPTX15-Sm2a

Summary for 6BL9

• Entry DOI: 10.2210/pdb6bl9/pdb
• NMR Information: BMRB: 30372
• Descriptor: Sm2a toxin (1 entity in total)
• Functional Keywords: scorpion toxin csab fold, toxin
• Biological source: Scolopendra morsitans
• Total number of polymer chains: 1
• Total formula weight: 6007.70

Authors

Harvey, P.J.,Craik, D.J.,Durek, T.,Dash, T.J. (deposition date: 2017-11-09, release date: 2018-11-14, Last modification date: 2024-11-06)

Primary citation

Dash, T.S.,Shafee, T.,Harvey, P.J.,Zhang, C.,Peigneur, S.,Deuis, J.R.,Vetter, I.,Tytgat, J.,Anderson, M.A.,Craik, D.J.,Durek, T.,Undheim, E.A.B.
A Centipede Toxin Family Defines an Ancient Class of CS alpha beta Defensins.
Structure, 27:315-326.e7, 2019

PubMed Abstract: Disulfide-rich peptides (DRPs) play diverse physiological roles and have emerged as attractive sources of pharmacological tools and drug leads. Here we describe the 3D structure of a centipede venom peptide, U-SLPTX-Sm2a, whose family defines a unique class of one of the most widespread DRP folds known, the cystine-stabilized α/β fold (CSαβ). This class, which we have named the two-disulfide CSαβ fold (2ds-CSαβ), contains only two internal disulfide bonds as opposed to at least three in all other confirmed CSαβ peptides, and constitutes one of the major neurotoxic peptide families in centipede venoms. We show the 2ds-CSαβ is widely distributed outside centipedes and is likely an ancient fold predating the split between prokaryotes and eukaryotes. Our results provide insights into the ancient evolutionary history of a widespread DRP fold and highlight the usefulness of 3D structures as evolutionary tools.

PubMed: 30554841
DOI: 10.1016/j.str.2018.10.022

Experimental method

SOLUTION NMR