2MUN
Solution structure of mu-SLPTX3-Ssm6a
Summary for 2MUN
| Entry DOI | 10.2210/pdb2mun/pdb |
| NMR Information | BMRB: 25223 |
| Descriptor | Mu-scoloptoxin-Ssm6a (1 entity in total) |
| Functional Keywords | toxin, mu-slptx-ssm6a, crustacean hyperglycemic hormone, ion channel inhibitor |
| Biological source | Scolopendra mutilans (Chinese red-headed centipede) |
| Cellular location | Secreted: P0DL36 |
| Total number of polymer chains | 1 |
| Total formula weight | 5333.00 |
| Authors | Undheim, E.A.B.,King, G.F.,Mobli, M. (deposition date: 2014-09-13, release date: 2015-06-24, Last modification date: 2023-06-14) |
| Primary citation | Undheim, E.A.,Grimm, L.L.,Low, C.F.,Morgenstern, D.,Herzig, V.,Zobel-Thropp, P.,Pineda, S.S.,Habib, R.,Dziemborowicz, S.,Fry, B.G.,Nicholson, G.M.,Binford, G.J.,Mobli, M.,King, G.F. Weaponization of a Hormone: Convergent Recruitment of Hyperglycemic Hormone into the Venom of Arthropod Predators. Structure, 23:1283-1292, 2015 Cited by PubMed Abstract: Arthropod venoms consist primarily of peptide toxins that are injected into their prey with devastating consequences. Venom proteins are thought to be recruited from endogenous body proteins and mutated to yield neofunctionalized toxins with remarkable affinity for specific subtypes of ion channels and receptors. However, the evolutionary history of venom peptides remains poorly understood. Here we show that a neuropeptide hormone has been convergently recruited into the venom of spiders and centipedes and evolved into a highly stable toxin through divergent modification of the ancestral gene. High-resolution structures of representative hormone-derived toxins revealed they possess a unique structure and disulfide framework and that the key structural adaptation in weaponization of the ancestral hormone was loss of a C-terminal α helix, an adaptation that occurred independently in spiders and centipedes. Our results raise a new paradigm for toxin evolution and highlight the value of structural information in providing insight into protein evolution. PubMed: 26073605DOI: 10.1016/j.str.2015.05.003 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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