Structure and mechanism of the lantibiotic cyclase involved in nisin biosynthesis.
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.
Li
Bo
B
Department of Biochemistry, University of Illinois at Urbana-Champaign, 600 South Mathews Avenue, Urbana, IL 61801, USA.
Yu
John Paul J
JP
Brunzelle
Joseph S
JS
Moll
Gert N
GN
van der Donk
Wilfred A
WA
Nair
Satish K
SK
D000595:Amino Acid Sequence; D000900:Anti-Bacterial Agents / Q000096:biosynthesis* / Q000737:chemistry; D013437:Carbon-Sulfur Lyases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D018360:Crystallography, X-Ray; D051231:Farnesyltranstransferase / Q000737:chemistry; D006801:Humans; D013294:Lactococcus lactis / Q000201:enzymology*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009561:Nisin / Q000096:biosynthesis* / Q000737:chemistry; D011487:Protein Conformation; D011499:Protein Processing, Post-Translational; D017386:Sequence Homology, Amino Acid; D013329:Structure-Activity Relationship
D000900:Anti-Bacterial Agents; D009561:Nisin; D051231:Farnesyltranstransferase; D013437:Carbon-Sulfur Lyases