1sn4
From Proteopedia
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|PDB= 1sn4 |SIZE=350|CAPTION= <scene name='initialview01'>1sn4</scene>, resolution 1.3Å | |PDB= 1sn4 |SIZE=350|CAPTION= <scene name='initialview01'>1sn4</scene>, resolution 1.3Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ACT:ACETATE ION'>ACT</scene> | + | |LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1sn1|1SN1]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1sn4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sn4 OCA], [http://www.ebi.ac.uk/pdbsum/1sn4 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1sn4 RCSB]</span> | ||
}} | }} | ||
| Line 27: | Line 30: | ||
[[Category: Wang, D C.]] | [[Category: Wang, D C.]] | ||
[[Category: Zeng, Z H.]] | [[Category: Zeng, Z H.]] | ||
| - | [[Category: ACT]] | ||
[[Category: neurotoxin]] | [[Category: neurotoxin]] | ||
[[Category: scorpion]] | [[Category: scorpion]] | ||
[[Category: sodium channel inhibitor]] | [[Category: sodium channel inhibitor]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:44:23 2008'' |
Revision as of 20:44, 30 March 2008
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| , resolution 1.3Å | |||||||
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| Ligands: | |||||||
| Related: | 1SN1
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF SCORPION NEUROTOXIN BMK M4
Overview
The crystal structures of two group III alpha-like toxins from the scorpion Buthus martensii Karsch, BmK M1 and BmK M4, were determined at 1.7 A and 1.3 A resolution and refined to R factors of 0.169 and 0.166, respectively. The first high-resolution structures of the alpha-like scorpion toxin show some striking features compared with structures of the "classical" alpha-toxin. Firstly, a non-proline cis peptide bond between residues 9 and 10 unusually occurs in the five-member reverse turn 8-12. Secondly, the cis peptide 9-10 mediates the spatial relationship between the turn 8-12 and the C-terminal stretch 58-64 through a pair of main-chain hydrogen bonds between residues 10 and 64 to form a unique tertiary arrangement which features the special orientation of the terminal residues 62-64. Finally, in consequence of the peculiar orientation of the C-terminal residues, the functional groups of Arg58, which are crucial for the toxin-receptor interaction, are exposed and accessible in BmK M1 and M4 rather than buried as in the classical alpha-toxins. Sequence alignment and characteristics analysis suggested that the above structural features observed in BmK M1 and M4 occur in all group III alpha-like toxins. Recently, some group III alpha-like toxins were demonstrated to occupy a receptor site different from the classical alpha-toxin. Therefore, the distinct structural features of BmK M1 and M4 presented here may provide the structural basis for the newly recognized toxin-receptor binding site selectivity. Besides, the non-proline cis peptide bonds found in these two structures play a role in the formation of the structural characteristics and in keeping accurate positions of the functionally crucial residues. This manifested a way to achieve high levels of molecular specificity and atomic precision through the strained backbone geometry.
About this Structure
1SN4 is a Single protein structure of sequence from Mesobuthus martensii. Full crystallographic information is available from OCA.
Reference
Crystal structures of two alpha-like scorpion toxins: non-proline cis peptide bonds and implications for new binding site selectivity on the sodium channel., He XL, Li HM, Zeng ZH, Liu XQ, Wang M, Wang DC, J Mol Biol. 1999 Sep 10;292(1):125-35. PMID:10493862
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