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The Gramicidin Pore: Crystal Structure of a Cesium Complex
Abstract
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.
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Cited by
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Physical properties of the fluid lipid-bilayer component of cell membranes: a perspective
Bloom, M., Evans, E., & Mouritsen, O. G. (1991) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583500003735 · Cited by 872
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Kagan, B. L., Selsted, M. E., Ganz, T., & Lehrer, R. I. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.1.210 · Cited by 532
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Hill, C. P., Yee, J., Selsted, M. E., & Eisenberg, D. (1991) · Science · doi:10.1126/science.2006422 · Cited by 507
Metadata
- Authors
- Wallace, B. A., & Ravikumar, K.
- Venue
- Science
- Published
- 1988-07-08
- Volume
- 241
- Issue
- 4862
- Pages
- 182-187
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2149995572
- Cited by
- 251
- References
- 0
- FWCI
- 5.97
- Type
- journal article
- Language
- en
- Open access
- closed
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