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Structure and Mechanism of the Lantibiotic Cyclase Involved in Nisin Biosynthesis
Bo Li,1*John Paul J. Yu,3*Joseph S. Brunzelle,4Gert N. Moll,5Wilfred A. van der Donk,1,2Satish K. Nair1,3
Nisin is a posttranslationally modified antimicrobial peptidethat is widely used as a food preservative. It contains fivecyclic thioethers of varying sizes that are installed by a singleenzyme, NisC. Reported here are the in vitro reconstitutionof the cyclization process and the x-ray crystal structure ofthe NisC enzyme. The structure reveals similarities in foldand substrate activation with mammalian farnesyl transferases,suggesting that human homologs of NisC posttranslationally modifya cysteine of a protein substrate.
1 Department of Biochemistry, University of Illinois at Urbana-Champaign, 600 South Mathews Avenue, Urbana, IL 61801, USA. 2 Department of Chemistry, University of Illinois at Urbana-Champaign, 600 South Mathews Avenue, Urbana, IL 61801, USA. 3 Center for Biophysics and Computational Biology, University of Illinois at Urbana-Champaign, 600 South Mathews Avenue, Urbana, IL 61801, USA. 4 Life Sciences Collaborative Access Team, Argonne National Labs, Argonne, IL, 60439, USA. 5 BiOMaDe Technology Foundation, Groningen, Netherlands.
* These authors contributed equally to this work.
To whom correspondence should be addressed. E-mail: vddonk{at}uiuc.edu (W.A.V.); s-nair{at}life.uiuc.edu (S.K.N)
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