PMID:10801488

Citation	Weber, T, Baumgartner, R, Renner, C, Marahiel, MA and Holak, TA (2000) Solution structure of PCP, a prototype for the peptidyl carrier domains of modular peptide synthetases. Structure 8:407-18
Abstract	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 domain (PCP) that passes the substrate to the reaction centres of the consecutive domains.
Links	PubMed
Keywords	Amino Acid Sequence; Binding Sites; Magnetic Resonance Spectroscopy; Models, Molecular; Molecular Sequence Data; Peptide Fragments/chemistry; Peptide Fragments/metabolism; Peptide Synthases/chemistry; Peptide Synthases/metabolism; Protein Conformation; Protein Structure, Tertiary; Sequence Homology, Amino Acid; Solutions
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