Four complete turns of a curved 310‐helix at atomic resolution: the crystal structure of the peptaibol trichovirin I‐4A in a polar environment suggests a transition to α‐helix for membrane function

$48.00 plus tax (Refund Policy)

Download / Buy Article:


The first crystal structure of a member of peptaibol antibiotic subfamily 4, trichovirin I‐4A (14 residues), has been determined by direct methods and refined at atomic resolution. The monoclinic unit cell has two molecules in the asymmetric unit. Both molecules assume a 310 right‐handed helical conformation and are significantly bent. The molecules pack loosely along the crystallographic twofold axis, forming two large tunnels between symmetry‐related molecules in which no ordered solvent could be located. Carbonyl O atoms which are not involved in intramolecular hydrogen bonding participate in close van der Waals interactions with apolar groups. The necessary amphipathicity for biological activity of peptaibols is not realised in the crystal structure. Hence, a structural change of trichovirin to an α‐helical conformation is proposed for membrane integration and efficient water/ion transportation across the lipid bilayer.

Document Type: Research Article


Publication date: February 1, 2012

Related content



Share Content

Access Key

Free Content
Free content
New Content
New content
Open Access Content
Open access content
Subscribed Content
Subscribed content
Free Trial Content
Free trial content
Cookie Policy
Cookie Policy
ingentaconnect website makes use of cookies so as to keep track of data that you have filled in. I am Happy with this Find out more