5EJD

The crystal structure of holo T3CT

Summary for 5EJD

• Entry DOI: 10.2210/pdb5ejd/pdb
• Descriptor: TqaA, GLYCEROL, 4'-PHOSPHOPANTETHEINE, ... (5 entities in total)
• Functional Keywords: biochemistry, enzyme, holo status, biosynthetic protein
• Biological source: Penicillium aethiopicum; More
• Total number of polymer chains: 16
• Total formula weight: 496242.31

Authors

Zhang, J.R.,Tang, Y.,Zhou, J.H. (deposition date: 2015-11-01, release date: 2016-10-19, Last modification date: 2024-04-24)

Primary citation

Zhang, J.,Liu, N.,Cacho, R.A.,Gong, Z.,Liu, Z.,Qin, W.,Tang, C.,Tang, Y.,Zhou, J.
Structural basis of nonribosomal peptide macrocyclization in fungi
Nat.Chem.Biol., 12:1001-1003, 2016

PubMed 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 (C) domain and the holo thiolation (T)-C 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.

PubMed: 27748753
DOI: 10.1038/nchembio.2202

Experimental method

X-RAY DIFFRACTION (2.49 Å)