5EJD

The crystal structure of holo T3CT

5EJD の概要

• エントリーDOI: 10.2210/pdb5ejd/pdb
• 分子名称: TqaA, GLYCEROL, 4'-PHOSPHOPANTETHEINE, ... (5 entities in total)
• 機能のキーワード: biochemistry, enzyme, holo status, biosynthetic protein
• 由来する生物種: Penicillium aethiopicum; 詳細
• タンパク質・核酸の鎖数: 16
• 化学式量合計: 496242.31

構造登録者

Zhang, J.R.,Tang, Y.,Zhou, J.H. (登録日: 2015-11-01, 公開日: 2016-10-19, 最終更新日: 2024-04-24)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.49 Å)