Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.
Active Motif, Inc.

Site Tools

  • AAAS
  • Subscribe
  • Feedback

Site Search

Search Advanced

Science 8 July 1988:
Vol. 241. no. 4862, pp. 182 - 187
DOI: 10.1126/science.2455344
Prev | Table of Contents | Next

Articles

Science, Vol 241, Issue 4862, 182-187
Copyright © 1988 by American Association for the Advancement of Science

articles

The gramicidin pore: crystal structure of a cesium complex

BA Wallace and K Ravikumar

Department of Chemistry and Center for Biophysics, Rensselaer Polytechnic Institute, Troy, NY 12180.

Gramicidin, a linear polypeptide composed of hydrophobic amino acids with alternating L- and D- configurations, forms transmembrane ion channels. The crystal structure of a gramicidin-cesium complex has been determined at 2.0 angstrom resolution. In this structure, gramicidin forms a 26 angstrom long tube comprised of two polypeptide chains arranged as antiparallel beta strands that are wrapped into a left-handed helical coil with 6.4 residues per turn. The polypeptide backbone forms the interior of the hydrophilic, solvent-filled pore and the side chains form a hydrophobic and relatively regular surface on the outside of the pore. This example of a crystal structure of a solvent-filled ion pore provides a basis for understanding the physical nature of ion translocation.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Monitoring Gramicidin Conformations in Membranes: A Fluorescence Approach.
S. S. Rawat, D. A. Kelkar, and A. Chattopadhyay (2004)
Biophys. J. 87, 831-843
   Abstract »    Full Text »    PDF »
Structural Restraints and Heterogeneous Orientation of the Gramicidin A Channel Closed State in Lipid Bilayers.
Y. Mo, T.A. Cross, and W. Nerdal (2004)
Biophys. J. 86, 2837-2845
   Abstract »    Full Text »    PDF »
Orientation and Lipid-Peptide Interactions of Gramicidin A in Lipid Membranes: Polarized Attenuated Total Reflection Infrared Spectroscopy and Spin-Label Electron Spin Resonance.
Z. Kota, T. Pali, and D. Marsh (2004)
Biophys. J. 86, 1521-1531
   Abstract »    Full Text »    PDF »
eSpectroscopic and Structural Properties of Valine Gramicidin A in Monolayers at the Air-Water Interface.
H. Lavoie, D. Blaudez, D. Vaknin, B. Desbat, B. M. Ocko, and C. Salesse (2002)
Biophys. J. 83, 3558-3569
   Abstract »    Full Text »    PDF »
The conducting form of gramicidin A is a right-handed double-stranded double helix.
B. M. Burkhart, N. Li, D. A. Langs, W. A. Pangborn, and W. L. Duax (1998)
PNAS 95, 12950-12955
   Abstract »    Full Text »    PDF »
High-resolution conformation of gramicidin A in a lipid bilayer by solid-state NMR.
R. Ketchem, W Hu, and T. Cross (1993)
Science 261, 1457-1460
   Abstract »    PDF »
Crystal structure of defensin HNP-3, an amphiphilic dimer: mechanisms of membrane permeabilization.
C. Hill, J Yee, M. Selsted, and D Eisenberg (1991)
Science 251, 1481-1485
   Abstract »    PDF »
Transmembrane channels based on tartaric acid-gramicidin A hybrids.
C. Stankovic, S. Heinemann, J. Delfino, F. Sigworth, and S. Schreiber (1989)
Science 244, 813-817
   Abstract »    PDF »
Structural polymorphism in transmembrane channels.
F. Salemme (1988)
Science 241, 145
   PDF »


ADVERTISEMENT
Click Me!

ADVERTISEMENT
Click Me!

To Advertise     Find Products

Science. ISSN 0036-8075 (print), 1095-9203 (online)