Structure and mechanism of the tRNA-dependent lantibiotic dehydratase NisB

Structural and biochemical studies show that the biosynthesis of the food preservative nisin involves the tRNA-dependent glutamylation of serine and threonine. Mechanisms of lantibiotic biosynthesis Nisin, a member of the lantibiotic family of thioether-bridge containing antibiotics, has been used w...

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Bibliographic Details
Published in:	Nature (London) Vol. 517; no. 7535; pp. 509 - 512
Main Authors:	Ortega, Manuel A., Hao, Yue, Zhang, Qi, Walker, Mark C., van der Donk, Wilfred A., Nair, Satish K.
Format:	Journal Article
Language:	English
Published:	London Nature Publishing Group UK 22.01.2015 Nature Publishing Group
Subjects:	631/45/173 631/535/1266 631/92/60 82/58 Analysis Antibiotics Bacterial Proteins - chemistry Bacterial Proteins - classification Bacterial Proteins - metabolism Bacteriocins - biosynthesis Bacteriocins - metabolism Bacteriology Biosynthesis Chemical properties Crystallography, X-Ray Dehydration E coli Enzymes Escherichia coli - genetics Food contamination Glutamic Acid - metabolism Gram-positive bacteria Health aspects Humanities and Social Sciences Hydro-Lyases - chemistry Hydro-Lyases - classification Hydro-Lyases - metabolism Lactococcus lactis - enzymology Lactococcus lactis - genetics letter Membrane Proteins - chemistry Membrane Proteins - classification Membrane Proteins - metabolism Models, Molecular multidisciplinary Nisin - biosynthesis Nisin - metabolism Peptides Phylogeny Physiological aspects Preservatives Protein Structure, Tertiary Proteins RNA, Transfer, Glu - genetics RNA, Transfer, Glu - metabolism Science Serine - metabolism Structure Threonine - metabolism Transfer RNA Massachusetts Illinois
ISSN:	0028-0836, 1476-4687, 1476-4687
Online Access:	Get full text
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