2G0D
Nisin cyclase
Summary for 2G0D
| Entry DOI | 10.2210/pdb2g0d/pdb |
| Related | 2GO2 |
| Descriptor | Nisin biosynthesis protein nisC, ZINC ION (3 entities in total) |
| Functional Keywords | alpha toroid, alpha barrel, biosynthetic protein |
| Biological source | Lactococcus lactis subsp. lactis |
| Total number of polymer chains | 1 |
| Total formula weight | 46857.91 |
| Authors | Nair, S.K. (deposition date: 2006-02-12, release date: 2006-05-23, Last modification date: 2024-02-14) |
| Primary citation | Li, B.,Yu, J.P.J.,Brunzelle, J.S.,Moll, G.N.,Van der Donk, W.A.,Nair, S.K. Structure and mechanism of the lantibiotic cyclase involved in nisin biosynthesis Science, 311:1464-1467, 2006 Cited by PubMed Abstract: 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. PubMed: 16527981DOI: 10.1126/science.1121422 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.21 Å) |
Structure validation
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