3TEJ

Crystal structure of a domain fragment involved in peptide natural product biosynthesis

3TEJ の概要

• エントリーDOI: 10.2210/pdb3tej/pdb
• 分子名称: Enterobactin synthase component F (2 entities in total)
• 機能のキーワード: nonribosomal peptide, thioesterase, carrier domain, atp- binding, enterobactin biosynthesis, ion transport, iron, iron transport, ligase, multifunctional enzyme, nucleotide- binding, phosphopantetheine, transferase, transport
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 72265.09

構造登録者

Liu, Y.,Zheng, T.,Bruner, S.D. (登録日: 2011-08-15, 公開日: 2012-01-18, 最終更新日: 2025-03-26)

主引用文献

Liu, Y.,Zheng, T.,Bruner, S.D.
Structural basis for phosphopantetheinyl carrier domain interactions in the terminal module of nonribosomal peptide synthetases.
Chem.Biol., 18:1482-1488, 2011

PubMed Abstract: Phosphopantetheine-modified carrier domains play a central role in the template-directed, biosynthesis of several classes of primary and secondary metabolites. Fatty acids, polyketides, and nonribosomal peptides are constructed on multidomain enzyme assemblies using phosphopantetheinyl thioester-linked carrier domains to traffic and activate building blocks. The carrier domain is a dynamic component of the process, shuttling pathway intermediates to sequential enzyme active sites. Here, we report an approach to structurally fix carrier domain/enzyme constructs suitable for X-ray crystallographic analysis. The structure of a two-domain construct of Escherichia coli EntF was determined with a conjugated phosphopantetheinyl-based inhibitor. The didomain structure is locked in an active orientation relevant to the chemistry of nonribosomal peptide biosynthesis. This structure provides details into the interaction of phosphopantetheine arm with the carrier domain and the active site of the thioesterase domain.

PubMed: 22118682
DOI: 10.1016/j.chembiol.2011.09.018

実験手法

X-RAY DIFFRACTION (1.9 Å)