3SBN

trichovirin I-4A in polar environment at 0.9 Angstroem

Summary for 3SBN

• Entry DOI: 10.2210/pdb3sbn/pdb
• Related PRD ID: PRD_000828
• Descriptor: Trichovirin I-4A, ACETONITRILE, METHANOL, ... (4 entities in total)
• Functional Keywords: curved 310-helix, 3-10 helix, peptide antibiotic, antibiotic
• Biological source: Hypocrea rufa (Trichoderma viride)
• Total number of polymer chains: 2
• Total formula weight: 2887.63

Authors

Gessmann, R.,Axford, D.,Petratos, K. (deposition date: 2011-06-06, release date: 2011-12-28, Last modification date: 2023-11-15)

Primary citation

Gessmann, R.,Axford, D.,Owen, R.L.,Bruckner, H.,Petratos, K.
Four complete turns of a curved 310-helix at atomic resolution: The crystal structure of the peptaibol trichovirin I-4A in polar environment suggests a transition to alpha-helix for membrane function
Acta Crystallogr.,Sect.D, 68:109-116, 2012

PubMed Abstract: 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.

PubMed: 22281739
DOI: 10.1107/S090744491105133X

Experimental method

X-RAY DIFFRACTION (0.9 Å)