CRYSTAL STRUCTURE OF NON-RIBOSOMAL PEPTIDE SYNTHETASES AND RELATED PROTEINS

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This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. The Non-Ribosomal Peptide Synthetases are modular, multidomain enzymes that synthesize peptides that frequently show antibiotic activity. These enzymes have multiple catalytic domains joined in an assembly line to catalyze the sequential elongation of the peptide product. We are interested in studying these proteins structurally to provide clues to how these distinct catalytic domains interact. Our studies are focused on the NRPS adenylation domains that bind to amino acids and covalently attach them to a pantetheine cofactor of an NRPS carrier protein domain. We wish to collect --higher resolution data to obtain a better model for the EntB protein --MAD data for the HBAL structure determination --high resolution data on several mutant enzymes of the CBAL to test the Domain Alternation hypothesis.