Structural highlights
Function
[NISC_LACLL] Could be implicated in the processing or the export process of the nisin lantibiotic.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Nisin is a posttranslationally modified antimicrobial peptide that is widely used as a food preservative. It contains five cyclic thioethers of varying sizes that are installed by a single enzyme, NisC. Reported here are the in vitro reconstitution of the cyclization process and the x-ray crystal structure of the NisC enzyme. The structure reveals similarities in fold and substrate activation with mammalian farnesyl transferases, suggesting that human homologs of NisC posttranslationally modify a cysteine of a protein substrate.
Structure and mechanism of the lantibiotic cyclase involved in nisin biosynthesis.,Li B, Yu JP, Brunzelle JS, Moll GN, van der Donk WA, Nair SK Science. 2006 Mar 10;311(5766):1464-7. PMID:16527981[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Li B, Yu JP, Brunzelle JS, Moll GN, van der Donk WA, Nair SK. Structure and mechanism of the lantibiotic cyclase involved in nisin biosynthesis. Science. 2006 Mar 10;311(5766):1464-7. PMID:16527981 doi:311/5766/1464
