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Crystal structure of the channel-forming polypeptide antiamoebin in a membrane-mimetic environment

Karle, Isabella L and Perozzo, Mary Ann and Mishra, Vinod K and Balaram, Padmanabhan (1998) Crystal structure of the channel-forming polypeptide antiamoebin in a membrane-mimetic environment. In: Proceedings of the National Academy of Sciences of the United States of America (PNAS), 95 (10). pp. 5501-5504.


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Crystals of an ion-channel-forming peptaibol peptide in a partial membrane environment have been obtained by cocrystallizing antiamoebin with n-octanol. The antiamoebin molecule has a bent helical conformation very similar to that established for Leu-zervamicin, despite a significantly different sequence for residues 1–8. The bent helices assemble to form a polar channel in the shape of an hour glass that is quite comparable to that of Leu-zervamicin. The molecules of cocrystallized octanol are found in two different areas with respect to the assembly of peptide molecules. One octanol molecule mimics a membrane segment along the hydrophobic exterior of the channel assembly. The other octanol molecules fill the channel in such a way that their OH termini satisfy the CAO moieties directed into the interior of the channel. Structure parameters for C82H27N17O20z3C8H18O are space group P212121, a = 9.143(2) Å, b = 28.590(8) Å, c = 44.289(8) Å, Z 5 4, agreement factor R1 5 11.95% for 4,113 observed ref lections [>4s(F)], resolution -1.0 Å.

Item Type: Journal Article
Additional Information: Copyright for this article belongs to National Academy of Sciences.
Department/Centre: Division of Biological Sciences > Molecular Biophysics Unit
Depositing User: M.K Anitha
Date Deposited: 04 Oct 2004
Last Modified: 19 Sep 2010 04:16
URI: http://eprints.iisc.ac.in/id/eprint/2081

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