Objective Non-ribosomal peptide synthetases (NRPSs) are a large family of modular multienzymes that catalyse the biosynthesis of many commercially important microbial natural products. Adenylation (A) domains within each NRPS module selectively bind and activate (by reaction with ATP) the amino acids constituting the peptide. Structure based models of A-domains have recently been developed, which identify potentially important residues for amino acid recognition and facilitate the prediction of new peptide natural pr oduct structures from genome sequence data. The accuracy of these structural predictions and the role played by putative recognition residues will be investigated using the Streptomyces coelicolor A3(2) coelichelin synthetase as a model. Fields of science natural sciencesbiological sciencesbiochemistrybiomoleculesnatural scienceschemical sciencesorganic chemistryaminesnatural sciencesbiological sciencesgeneticsgenomes Keywords Peptide siderophore Streptomyces genomics Programme(s) FP6-MOBILITY - Human resources and Mobility in the specific programme for research, technological development and demonstration "Structuring the European Research Area" under the Sixth Framework Programme 2002-2006 Topic(s) MOBILITY-2.1 - Marie Curie Intra-European Fellowships (EIF) Call for proposal FP6-2002-MOBILITY-5 See other projects for this call Funding Scheme EIF - Marie Curie actions-Intra-European Fellowships Coordinator UNIVERSITY OF WARWICK Address Gibbet hill road Coventry United Kingdom See on map EU contribution € 0,00
