2a7t
From Proteopedia
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'''Crystal Structure of a novel neurotoxin from Buthus tamalus at 2.2A resolution.''' | '''Crystal Structure of a novel neurotoxin from Buthus tamalus at 2.2A resolution.''' | ||
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[[Category: Srinivasan, A.]] | [[Category: Srinivasan, A.]] | ||
[[Category: Yadav, S.]] | [[Category: Yadav, S.]] | ||
| - | [[Category: | + | [[Category: Crystal structure]] |
| - | [[Category: | + | [[Category: Neurotoxin]] |
| - | [[Category: | + | [[Category: Novel]] |
| - | [[Category: | + | [[Category: Red scorpion]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 18:43:07 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 15:43, 3 May 2008
Crystal Structure of a novel neurotoxin from Buthus tamalus at 2.2A resolution.
Overview
The crystal structure of a highly acidic neurotoxin from the scorpion Buthus tamulus has been determined at 2.2A resolution. The amino acid sequence determination shows that the polypeptide chain has 64 amino acid residues. The pI measurement gave a value of 4.3 which is one of the lowest pI values reported so far for a scorpion toxin. As observed in other alpha-toxins, it contains four disulphide bridges, Cys12-Cys63, Cys16-Cys36, Cys22-Cys46, and Cys26-Cys48. The crystal structure reveals the presence of two crystallographically independent molecules in the asymmetric unit. The conformations of two molecules are identical with an r.m.s. value of 0.3A for their C(alpha) tracings. The overall fold of the toxin is very similar to other scorpion alpha-toxins. It is a betaalphabetabeta protein. The beta-sheet involves residues Glu2-Ile6 (strand beta1), Asp32-Trp39 (strand beta3) and Val45-Val55 (strand beta4). The single alpha-helix formed is by residues Asn19-Asp28 (alpha2). The structure shows a trans peptide bond between residues 9 and 10 in the five-membered reverse turn Asp8-Cys12. This suggests that this toxin belongs to classical alpha-toxin subfamily. The surface features of the present toxin are highly characteristic, the first (A-site) has residues, Phe18, Trp38 and Trp39 that protrude outwardly presumably to interact with its receptor. There is another novel face (N-site) of this neurotoxin that contains several negatively charged residues such as, Glu2, Asp3, Asp32, Glu49 and Asp50 which are clustered in a small region of the toxin structure. On yet another face (P-site) in a triangular arrangement, with respect to the above two faces there are several positively charged residues, Arg58, Lys62 and Arg64 that also protrude outwardly for a potentially potent interaction with other molecules. This toxin with three strong features appears to be one of the most toxic molecules reported so far. In this sense, it may be a new subclass of neurotoxins with the largest number of hot spots.
About this Structure
2A7T is a Single protein structure of sequence from Mesobuthus tamulus. Full crystallographic information is available from OCA.
Reference
Crystal structure of a highly acidic neurotoxin from scorpion Buthus tamulus at 2.2A resolution reveals novel structural features., Sharma M, Ethayathulla AS, Jabeen T, Singh N, Sarvanan K, Yadav S, Sharma S, Srinivasan A, Singh TP, J Struct Biol. 2006 Jul;155(1):52-62. Epub 2006 Jan 9. PMID:16677826 Page seeded by OCA on Sat May 3 18:43:07 2008
