2sn3 | pdb_00002sn3

STRUCTURE OF SCORPION TOXIN VARIANT-3 AT 1.2 ANGSTROMS RESOLUTION

spinqualitylabelsall models 2sn3, resolution 1.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2sn3 is a 1 chain structure with sequence from Bark scorpion. This structure supersedes the now removed PDB entry 1sn3. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: MPD Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [SCX3_CENSC] Beta toxins bind voltage-independently at site-4 of sodium channels (Nav) and shift the voltage of activation toward more negative potentials thereby affecting sodium channel activation and promoting spontaneous and repetitive firing (By similarity). Induces immediate paralysis in crickets after injection, with a total paralysis occurring within 15-30 minutes and lasting for 1-2 hours. Is also lethal to vertebrate (chicks) when injected in very high dosages (more that 100 mg/kg). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The crystal structure of the variant-3 protein neurotoxin from the scorpion Centruroides sculpturatus Ewing has been refined at 1.2 A resolution using restrained least-squares. The final model includes 492 non-hydrogen protein atoms, 453 protein hydrogen atoms, eight 2-methyl-2,4-pentanediol (MPD) solvent atoms, and 125 water oxygen atoms. The variant-3 protein model geometry deviates from ideal bond lengths by 0.024 A and from ideal angles by 3.6 degrees. The crystallographic R-factor for structure factors calculated from the final model is 0.192 for 17,706 unique reflections between 10.0 to 1.2 A. A comparison between the models of the initial 1.8 A and the 1.2 A refinement shows a new arrangement of the previously poorly defined residues 31 to 34. Multiple conformations are observed for four cysteine residues and an MPD oxygen atom. The electron density indicates that disulfide bonds between Cys12 and Cys65 and between Cys29 and Cys48 have two distinct side-chain conformations. A molecule of MPD bridges neighboring protein molecules in the crystal lattice, and both MPD enantiomers are present in the crystal. A total of 125 water molecules per molecule of protein are included in the final model with B-values ranging from 11 to 52 A2 and occupancies from unity down to 0.4. Comparisons between the 1.2 A and 1.8 A models, including the bound water structure and crystal packing contacts, are emphasized. Structure of scorpion toxin variant-3 at 1.2 A resolution.,Zhao B, Carson M, Ealick SE, Bugg CE J Mol Biol. 1992 Sep 5;227(1):239-52. PMID:1522588 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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