Title: Structure of the ion channel peptide antibiotic gramicidin A
Abstract: Abstract The crystal structure of the uncomplexed orthorhombic form of gramicidin A has been determined at 0.86 Å resolution. The polypeptide crystallizes from ethanol as a left‐handed, double‐stranded, antiparallel β 5.6 ‐helical dimer that is 31 Å long and an average of 4.8 Å in diameter. The uncomplexed channel does not contain ions or solvent molecules, and its diameter is not uniform but varies from a minimum of 3.85 Å to a maximum of 5.47 Å. There are three empty cavities in the channel that have a diameter exceeding 5.25 Å and appear to be large enough to accommodate water molecules or potassium ions in a chemically reasonable coordination environment. The observed crystal structure does not offer any obvious clues as to why an antiparallel β 5.6 ‐helix cannot function as an ion channel in lipid bilayers.
Publication Year: 1989
Publication Date: 1989-01-01
Language: en
Type: article
Indexed In: ['crossref', 'pubmed']
Access and Citation
Cited By Count: 22
AI Researcher Chatbot
Get quick answers to your questions about the article from our AI researcher chatbot