1WM7

Solution Structure of BmP01 from the Venom of Scorpion Buthus martensii Karsch, 9 structures

Summary for 1WM7

• Entry DOI: 10.2210/pdb1wm7/pdb
• Related: 1ACW 1DU9 1PNH 1SCY
• Descriptor: Neurotoxin BmP01 (1 entity in total)
• Functional Keywords: alpha/beta scaffold, toxin
• Biological source: Mesobuthus martensii (Chinese scorpion)
• Cellular location: Secreted: Q9U8D2
• Total number of polymer chains: 1
• Total formula weight: 3188.57

Authors

Wu, G.,Li, Y.,Wei, D.,He, F.,Jiang, S.,Hu, G.,Wu, H.,Chen, X. (deposition date: 2004-07-05, release date: 2004-07-27, Last modification date: 2022-03-02)

Primary citation

Wu, G.,Li, Y.,Wei, D.,He, F.,Jiang, S.,Hu, G.,Wu, H.
Solution Structure of BmP01 from the Venom of Scorpion Buthus martensii Karsch
Biochem.Biophys.Res.Commun., 276:1148-1154, 2000

PubMed Abstract: From the venom of scorpion Buthus martensii Karsch,a short peptide (BmP01, 29 amino acid residues) was isolated and characterized as previously reported (Lebren, R. R., et al. (1997) Eur. J. Biochem. 245, 457-464). It was shown to reduce 33% outward K(+) channel (hippocampal neurons) currents at 10 microM. The solution structure of BmP01 was determined by 2D (1)H NMR spectroscopy. The NOEs, coupling constants, and H-D exchange obtained from NMR spectroscopy were used in structural calculations. The conformation of BmP01 is composed of a short alpha-helix (Cys 3-Thr 12) and a two-stranded antiparallel beta-sheet (Ala 15-Asp 20 and Lys 23-Pro 28). There are three disulfide bridges (Cys 3-Cys 19, Cys 6-Cys 24 and Cys 10-Cys 26) connecting the alpha-helix and beta-sheet. Asp 20 to Lys 23 form a type II turn linking the two strands. Structural and electrostatic potential comparison between BmP01 and its analogues are also presented.

PubMed: 11027603
DOI: 10.1006/bbrc.2000.3435

Experimental method

SOLUTION NMR