1vib
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1vib |SIZE=350|CAPTION= <scene name='initialview01'>1vib</scene> | |PDB= 1vib |SIZE=350|CAPTION= <scene name='initialview01'>1vib</scene> | ||
|SITE= | |SITE= | ||
| - | |LIGAND= | + | |LIGAND= <scene name='pdbligand=HYP:4-HYDROXYPROLINE'>HYP</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1vib FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vib OCA], [http://www.ebi.ac.uk/pdbsum/1vib PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1vib RCSB]</span> | ||
}} | }} | ||
| Line 30: | Line 33: | ||
[[Category: toxin]] | [[Category: toxin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:24:51 2008'' |
Revision as of 21:24, 30 March 2008
| |||||||
| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
NMR SOLUTION STRUCTURE OF THE NEUROTOXIN B-IV, 20 STRUCTURES
Overview
B-IV is a 55-residue, crustacean-selective, neurotoxin secreted by Cerebratulus lacteus, a large marine worm found along the northeastern coast of North America. The 3D structure of this molecule in aqueous solution has been determined by 1H NMR spectroscopy at 600 MHz. The molecule has a well-defined helical hairpin structure, with the branches of the hairpin linked by four disulphide bonds. The disulphide connectivities were established from the NMR data to be 1-8/2-7/3-6/4-5, which differed from those determined previously by chemical means, where 1-7 and 2-8 connectivities were found. Each branch of the hairpin is largely alpha-helical, with the helices in the N and C-terminal branches encompassing residues 11 to 23 and 34 to 49, respectively. The loop connecting the branches of the hairpin contains two inverse gamma-turns centred on residues 24 and 25, a type I beta-turn at residues 28 to 31 and a type II beta-turn at residues 30 to 33. Arg17, -25 and -34, which are important for activity, are all on the same face of the molecule, while Trp30, which is also important for activity, is on the opposite face. Structure comparisons show that the B-IV structure is quite similar to those of Rop (ColE1 repressor of primer) and the heat-stable enterotoxin B from Escherichia coli. These structural similarities are discussed in relation to possible mechanisms of action of B-IV.
About this Structure
1VIB is a Single protein structure of sequence from Cerebratulus lacteus. Full crystallographic information is available from OCA.
Reference
Structure of neurotoxin B-IV from the marine worm Cerebratulus lacteus: a helical hairpin cross-linked by disulphide bonding., Barnham KJ, Dyke TR, Kem WR, Norton RS, J Mol Biol. 1997 May 23;268(5):886-902. PMID:9180379
Page seeded by OCA on Mon Mar 31 00:24:51 2008
