1wt8: Difference between revisions

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|ACTIVITY=  
|ACTIVITY=  
|GENE=  
|GENE=  
|DOMAIN=
|RELATEDENTRY=[[1acw|1ACW]], [[1du9|1DU9]], [[1pnh|1PNH]], [[1scy|1SCY]]
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1wt8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wt8 OCA], [http://www.ebi.ac.uk/pdbsum/1wt8 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1wt8 RCSB]</span>
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[[Category: alpha/beta scaffold]]
[[Category: alpha/beta scaffold]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:01:11 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:40:39 2008''

Revision as of 00:40, 31 March 2008

File:1wt8.gif


PDB ID 1wt8

Drag the structure with the mouse to rotate
Related: 1ACW, 1DU9, 1PNH, 1SCY


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Solution Structure of BmP08 from the Venom of Scorpion Buthus martensii Karsch, 20 structures


OverviewOverview

A novel short-chain scorpion toxin BmP08 was purified from the venom of the Chinese scorpion Buthus martensi Karsch by a combination of gel-filtration, ion exchange, and reversed-phase chromatography. The primary sequence of BmP08 was determined using the tandem MS/MS technique and Edman degradation, as well as results of NMR sequential assignments. It is composed of 31 amino acid residues including six cysteine residues and shares less than 25% sequence identity with the known alpha-KTx toxins. BmP08 shows no inhibitory activity on all tested voltage-dependent and Ca(2+)-activated potassium channels. The 3D-structure of BmP08 has been determined by 2D-NMR spectroscopy and molecular modeling techniques. This toxin adopts a common alpha/beta-motif, but shows a distinctive local conformation and features a 3(10)-helix and a shorter beta-sheet. The unique structure is closely related to the distinct primary sequence of the toxin, especially to the novel arrangement of S-S linkages in the molecule, in which two disulfide bridges (C(i)-C(j) and C(i+3)-C(j+3)) link covalently the 3(10)-helix with one strand of the beta-sheet structure. The electrostatic potential surface analysis of the toxin reveals salt bridges and hydrogen bonds between the basic residues and negatively charged residues nearby in BmP08, which may be unfavorable for its binding with the known voltage-dependent and Ca(2+)-activated potassium channels. Thus, finding the target for this toxin should be an interesting task in the future.

About this StructureAbout this Structure

1WT8 is a Single protein structure of sequence from Mesobuthus martensii. Full crystallographic information is available from OCA.

ReferenceReference

Solution structure of BmP08, a novel short-chain scorpion toxin from Buthus martensi Karsch., Chen X, Li Y, Tong X, Zhang N, Wu G, Zhang Q, Wu H, Biochem Biophys Res Commun. 2005 May 20;330(4):1116-26. PMID:15823559

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