Solution structure of PCP, a prototype for the peptidyl carrier domains of modular peptide synthetases.

@article{Weber2000SolutionSO,
  title={Solution structure of PCP, a prototype for the peptidyl carrier domains of modular peptide synthetases.},
  author={Till Weber and Roland Baumgartner and Christian Renner and Mohamed A. Marahiel and Tad A. Holak},
  journal={Structure},
  year={2000},
  volume={8 4},
  pages={407-18}
}
BACKGROUND Nonribosomal peptide synthetases (NRPSs) are large modular enzymes responsible for the synthesis of a variety of microbial bioactive peptides. They consist of modules that each recognise and incorporate one specific amino acid into the peptide product. A module comprises several domains, which carry out the individual reaction steps. After activation by the adenylation domain, the amino acid substrate is covalently tethered to a 4'-phosphopantetheinyl cofactor of a peptidyl carrier… CONTINUE READING

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