6AD3

Structural characterization of the condensation domain from Monacolin K polyketide synthase MokA

6AD3 の概要

• エントリーDOI: 10.2210/pdb6ad3/pdb
• 分子名称: Lovastatin nonaketide synthase mokA (2 entities in total)
• 機能のキーワード: polyketide synthease, condensation domain, nonribosomal peptide synthetases, biosynthetic protein
• 由来する生物種: Monascus pilosus (Red mold)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 57446.18

構造登録者

Wang, L.,Zheng, J. (登録日: 2018-07-30, 公開日: 2019-04-03, 最終更新日: 2024-03-27)

主引用文献

Wang, L.,Yuan, M.,Zheng, J.
Crystal structure of the condensation domain from lovastatin polyketide synthase.
Synth Syst Biotechnol, 4:10-15, 2019

PubMed Abstract: The highly reducing iterative polyketide synthases responsible for lovastatin biosynthesis contains a section homologous to condensation (CON) domain observed in nonribosomal peptide synthetases (NRPSs). In the present study, we expressed the isolated lovastatin CON domain and solved the crystal structure to 1.79 Å resolution. The overall structure shows similarity to canonical condensation domains of NRPSs, containing the N-terminal and C-terminal subdomains that resemble enzymes of chloramphenicol acetyltransferase family, whereas distinct structural features are observed at the active site. The acceptor entry of the substrate channel is blocked by a flexible loop, thereby preventing the loading of substrate for a new round of chain elongation. The mutation of conserved catalytic motif located at the midpoint of substrate channel agrees with the incapability of CON to catalyzed amide-bond formation. The structure helps to understand the function of CON in lovastatin biosynthesis.

PubMed: 30533541
DOI: 10.1016/j.synbio.2018.11.003

実験手法

X-RAY DIFFRACTION (1.79 Å)