Crystal structure of [Leu1]zervamicin, a membran ion-channel peptide: Implications for gating mechanisms

Karle, Isabella L and Flippen-Anderson, Judith L and Agarwalla, Sanjay and Balaram, Padmanabhan (1991) Crystal structure of [Leu1]zervamicin, a membran ion-channel peptide: Implications for gating mechanisms. In: Proceedings of the National Academy of Sciences of the United States of America, 88 (12). pp. 5307-5311.

PDF crystal.pdf Restricted to Registered users only Download (891kB) | Request a copy

Abstract

Structures in four different crystal forms of [Leu1]zervamicin (zervamicin Z-L, Ac-Leu-Ile-Gln-Iva-Ile5-Thr-Aib-Leu-Aib-Hyp10-Gln-Aib -Hyp-Aib- Pro15-Phol, where Iva is isovaline, Aib is \alpha-amino isobutyric acid, Hyp is 4-hydroxyproline, and Phol is phenylalaninol), a membrane channel-forming polypeptide from Emericellopsis salmosynnemata, have been determined by x-ray diffraction. The helical structure is amphiphilic with all the polar moieties on the convex side of the bent helix. Helices are bent at Hyp10 from \approx 30 deg to \approx 45 deg in the different crystal forms. In all crystal forms, the peptide helices aggregate in a similar fashion to form water channels that are interrupted by hydrogen bonds between N H(Gln11) and O \delta (Hyp10) of adjacent helices. The Gln11 side chain is folded in an unusual fashion in order to close the channel. Space is available for an extended conformation for Gln11, in which case the channel would be open, suggesting a gating mechanism for cation transport. Structural details are presented for one crystal form derived from methanol/water solution: C85H140N18O22. 10H2O, space group P21, a = 23.068(6) A, b = 9.162(3) A, c = 26.727(9) A, \beta = 108.69(2) (standard deviation of last digit is given in parentheses); overall agreement factor R = 10.1% for 5322 observed reflections [|Fo| > 3\sigma (F)]; resolution, 0.93 A.

Item Type:	Journal Article
Publication:	Proceedings of the National Academy of Sciences of the United States of America
Publisher:	National Academy of Sciences
Additional Information:	Copyright for this article belongs to National Academy of Sciences.
Keywords:	X-ray diffraction;channel mouth;helix bending;polymorphs;alpha-alkyl amino acid
Department/Centre:	Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited:	23 Dec 2004
Last Modified:	19 Sep 2010 04:17
URI:	http://eprints.iisc.ac.in/id/eprint/2511

Actions (login required)

View Item