Letter | Published:

A novel conformation of valinomycin in its barium complex

Nature volume 286, pages 640641 (07 August 1980) | Download Citation

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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.

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  1. Molecular Biophysics Unit, Indian Institute of Science, Bangalore-560 012, India

    • S. Devarajan
    • , C. M. K. Nair
    • , K. R. K. Easwaran
    •  & M. Vijayan

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DOI

https://doi.org/10.1038/286640a0

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