A novel conformation of valinomycin in its barium complex
- 1 August 1980
- journal article
- letter
- Published by Springer Nature in Nature
- Vol. 286 (5773) , 640-641
- https://doi.org/10.1038/286640a0
Abstract
Knowledge of the molecular mechanisms involved in ionophore-mediated cation transport would be valuable for under-standing many essential functions of biological membranes1–3. Cations are transported in several stages, such as formation of the ionophore–cation complex, diffusion across the cell membrane and subsequent release of the cation. Several conformational rearrangements are involved in this process, and so a detailed understanding of all the conformational possibilities of the ionophore seems to be essential for elucidating the molecular mechanism of ion transport. We are carrying out spectroscopic and crystallographic studies to explore the possible conformational stages of ionophores by complexing them, in different solvents, with cations of various sizes and charges. We report here a novel conformation of the ionophore valinomycin in its barium complex. It can be described as an extended depsipeptide chain, without internal hydrogen bonds, wound in the form of an ellipse with the two barium ions located at the foci.Keywords
This publication has 5 references indexed in Scilit:
- Physico‐chemical Basis of Ion Transport through Biological Membranes: Ionophores and Ion ChannelsEuropean Journal of Biochemistry, 1979
- Biological Applications of IonophoresAnnual Review of Biochemistry, 1976
- Crystal and molecular structure of the triclinic and monoclinic forms of valinomycin, C54H90N6O18Journal of the American Chemical Society, 1975
- Conformation of valinomycin in a triclinic crystal formJournal of the American Chemical Society, 1975
- The Crystal Structure of a K+ Complex of ValinomycinHelvetica Chimica Acta, 1975