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NMR Studies of Lantibiotics: The Three-Dimensional Structure of Nisin in Aqueous Solution

  • Conference paper
Bacteriocins, Microcins and Lantibiotics

Part of the book series: NATO ASI Series ((ASIH,volume 65))

Summary

Nisin, a bacteriocin produced by Lactococcus lactis ssp., is a post-translationally modified pentacyclic polypeptide of 34 amino acids. It is a member of the class of bacteriocins, known as lantibiotics, that contain the unusual amino acid lanthionine. Its structure in aqueous solution has been determined on the basis of data obtained from Nuclear Magnetic Resonance Spectroscopy (NMR) studies. Translation of the interproton distance constraints, derived from Nuclear Overhauser Enhancement Spectroscopy (NOESY)l, and torsion angle constraints, derived from Double Quantum Filtered Correlated Spectroscopy (DQF-COSY), into a 3D structure was carried out with the distance geometry program DISMAN, followed by restrained energy minimization using CHARMm. Due to the internal mobility of the polypeptide chain a determination of the precise overal folding of the molecule was prohibited, but parts of the structure could be obtained albeit with sometimes low resolution. The structure of nisin can best be described as follows: the outermost N-and C-terminal regions appear quite flexible, the remainder of the molecule consists of an amphiphilic N-terminal fragment (residues 3–19), joined by a flexible ‘hinge’ region to a rigid doublering fragment formed by residues 23–28. The latter fragment has the appearance of a somewhat overwound α-helix. It is postulated that i) the coupling between residues 23 and 26 as well as between 25 and 28 by thioether bridges and ii) the inversion of the Cα chiralities at positions 23 and 25 occurs via an intermediate α-helical structure of the prenisin molecule

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Abbreviations

NOESY:

Nuclear Overhauser Enhancement Spectroscopy

COSY:

Correlated Spectroscopy

DQF:

Double Quantum Filter

Dhb(O):

Dehydrobutyrine (β-methyldehydroalanine)

Dha (U):

dehydroalanine

Alas :

alanine moiety of lanthionine

D-Abu:

β-methylalanine moiety of β-mehyllanthionine

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Authors and Affiliations

  1. Nijmegen SON Research Center Laboratory of Biophysical Chemistry, University of Nijmegen, 6525 ED, Nijmegen, Toernooiveld, The Netherlands

    Frank J. M. van de Ven, Henno W. van den Hooven, Cornelis W. Hilbers & Ruud N. H. Konings

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  1. Frank J. M. van de Ven
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  2. Henno W. van den Hooven
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  3. Cornelis W. Hilbers
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  4. Ruud N. H. Konings
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Editor information

Editors and Affiliations

  1. School of Biological Sciences, University of East Anglia, Norwich, Norfolk, NR4 7TJ, UK

    Richard James

  2. Centre National de la Recherche Scientifique, Centre de Biochimie et de Biologie Moléculaire, 31, chemin Joseph Aiguier, B. P. 71, 13402, Marseille Cédex 9, France

    Claude Lazdunski

  3. European Molecular Biology Laboratory, Meyerhofstrasse 1, Postfach 10 22 09, 6900, Heidelberg, Germany

    Franc Pattus

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© 1992 Springer-Verlag Berlin Heidelberg

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van de Ven, F.J.M., van den Hooven, H.W., Hilbers, C.W., Konings, R.N.H. (1992). NMR Studies of Lantibiotics: The Three-Dimensional Structure of Nisin in Aqueous Solution. In: James, R., Lazdunski, C., Pattus, F. (eds) Bacteriocins, Microcins and Lantibiotics. NATO ASI Series, vol 65. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-76974-0_39

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  • DOI: https://doi.org/10.1007/978-3-642-76974-0_39

  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-642-76976-4

  • Online ISBN: 978-3-642-76974-0

  • eBook Packages: Springer Book Archive

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