1chz
From Proteopedia
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A NEW NEUROTOXIN FROM BUTHUS MARTENSII KARSCH
Overview
A new neurotoxin BmK M2, toxic to both mammals and insects, with the, strongest toxicity in the BmK toxin series, has been purified from the, Chinese scorpion Buthus martensii Karsch and crystallized with MPD at pH, 7.5. The crystals are orthorhombic, belonging to space group, P2(1)2(1)2(1), with unit-cell parameters a = 36.64, b = 36.95, c = 37.23, A. The structure was solved by molecular replacement and refined to R =, 0.186 for all reflections to a resolution of 1.76 A. The whole sequence, (64 residues) of BmK M2 was determined by crystallographic analysis based, on high-resolution data and the homologous model of BmK M8. The refined, BmK M2 structure shows a non-proline cis peptide bond between Pro9 and, His10 which enables the C-terminal segment to adopt a conformation, different to that of the weak toxin BmK M8. Recently, a mutation analysis, had suggested that both the tenth residue and the C-terminus play key, roles in receptor binding. Therefore, these features may be related to the, binding selectivity of the group III alpha-like toxins. The charge changes, of residues 8, 10, 18, 28, 55 and 59 from neutral or negative to positive, or neutral, which leads to a positive electrostatic potential surface, may, be responsible for the high toxicity of BmK M2.
About this Structure
1CHZ is a Single protein structure of sequence from Mesobuthus martensii with CL as ligand. Full crystallographic information is available from OCA.
Reference
Structure of a new neurotoxin from the scorpion Buthus martensii Karsch at 1.76 A., He XL, Deng JP, Wang M, Zhang Y, Wang DC, Acta Crystallogr D Biol Crystallogr. 2000 Jan;56(Pt 1):25-33. PMID:10666623
Page seeded by OCA on Tue Nov 20 12:28:25 2007
Categories: Mesobuthus martensii | Single protein | Deng, J.P. | He, X.L. | Li, H.M. | Wang, D.C. | CL | Neurotoxin | Scorpion
