Crystal and molecular structure of the membrane-active antibiotic enniatin C

Abstract

The crystal structure of the cyclic hexadepsipeptide antibiotic enniatin Cc[-(L-MeLeu-D-Hyi)3-], C34H59N3O9, was established by X-ray structure analysis (sp. gr. P21, a = 20.205(5) A, b = 8.702(2) A, c = 25.587(6) A, γ = 97.0(5)°, V = 4465.3(18) A3, Z = 4, R = 0.089 for 3601 reflections with I > 2σ(I)). The unit cell contains two independent molecules of enniatin C, one ethanol molecule disordered over two positions, and approximately two water molecules occupying four positions and forming hydrogen bonds with each other. The independent antibiotic molecules adopt virtually identical conformations similar to those observed in the structures of enniatin B and its Na,Ni-complex. These conformations are characterized by alternating upward and downward orientations of the carbonyl groups and pseudoequatorial orientations of side radicals. The Leu residues have stretched conformations. The N-methylamide groups of the independent antibiotic molecules face each other, whereas the molecules are displaced by approximately 8.4 A with respect to each other along the mean planes of the rings.