4KYP

Beta-Scorpion Toxin folded in the periplasm of E.coli

Summary for 4KYP

Entry DOI	10.2210/pdb4kyp/pdb
Related	1BCG
Descriptor	Beta-insect excitatory toxin Bj-xtrIT, TRIETHYLENE GLYCOL, TETRAETHYLENE GLYCOL, ... (4 entities in total)
Functional Keywords	alpha-beta, venom, voltage gated na-channels, toxin
Biological source	Hottentotta judaicus (Scorpion)
Cellular location	Secreted: P56637
Total number of polymer chains	4
Total formula weight	38253.16
Authors	O'Reilly, A.O.,Cole, A.R.,Lopes, J.L.,Lampert, A.,Wallace, B.A. (deposition date: 2013-05-29, release date: 2014-02-12, Last modification date: 2018-01-24)
Primary citation	O'Reilly, A.O.,Cole, A.R.,Lopes, J.L.,Lampert, A.,Wallace, B.A. Chaperone-mediated native folding of a beta-scorpion toxin in the periplasm of Escherichia coli. Biochim.Biophys.Acta, 1840:10-15, 2014 Cited by PubMed Abstract: Animal neurotoxin peptides are valuable probes for investigating ion channel structure/function relationships and represent lead compounds for novel therapeutics and insecticides. However, misfolding and aggregation are common outcomes when toxins containing multiple disulfides are expressed in bacteria. PubMed: 23999087 DOI: 10.1016/j.bbagen.2013.08.021 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.7 Å)

Structure validation