1DNY

SOLUTION STRUCTURE OF PCP, A PROTOTYPE FOR THE PEPTIDYL CARRIER DOMAINS OF MODULAR PEPTIDE SYNTHETASES

Summary for 1DNY

• Entry DOI: 10.2210/pdb1dny/pdb
• Descriptor: NON-RIBOSOMAL PEPTIDE SYNTHETASE PEPTIDYL CARRIER PROTEIN (1 entity in total)
• Functional Keywords: four-helix bundle, modular enzyme, flexible region, 4'-phosphopantetheinyl cofactor, modular peptide synthetases, nonribosomal peptide synthesis, peptidyl carrier protein (pcp), ligase
• Biological source: Brevibacillus brevis
• Total number of polymer chains: 1
• Total formula weight: 10119.62

Authors

Weber, T.,Baumgartner, R.,Renner, C.,Marahiel, M.A.,Holak, T.A. (deposition date: 1999-12-17, release date: 2000-05-17, Last modification date: 2024-05-22)

Primary citation

Weber, T.,Baumgartner, R.,Renner, C.,Marahiel, M.A.,Holak, T.A.
Solution structure of PCP, a prototype for the peptidyl carrier domains of modular peptide synthetases.
Structure Fold.Des., 8:407-418, 2000

PubMed 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.

PubMed: 10801488
DOI: 10.1016/S0969-2126(00)00120-9

Experimental method

SOLUTION NMR