| Literature DB >> 27748753 |
Nicholas Liu1, Ralph A Cacho1, Jinru Zhang2, Zhou Gong3, Zhu Liu4, Wenming Qin5, Chun Tang3,4, Yi Tang1, Jiahai Zhou2,6.
Abstract
Nonribosomal peptide synthetases (NRPSs) in fungi biosynthesize important pharmaceutical compounds, including penicillin, cyclosporine and echinocandin. To understand the fungal strategy of forging the macrocyclic peptide linkage, we determined the crystal structures of the terminal condensation-like (CT) domain and the holo thiolation (T)-CT complex of Penicillium aethiopicum TqaA. The first, to our knowledge, structural depiction of the terminal module in a fungal NRPS provides a molecular blueprint for generating new macrocyclic peptide natural products.Entities:
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Year: 2016 PMID: 27748753 PMCID: PMC5110376 DOI: 10.1038/nchembio.2202
Source DB: PubMed Journal: Nat Chem Biol ISSN: 1552-4450 Impact factor: 15.040