5IG8

Crystal structure of macrocyclase MdnB from Microcystis aeruginosa MRC

5IG8 の概要

• エントリーDOI: 10.2210/pdb5ig8/pdb
• 関連するPDBエントリー: 5IG9
• 分子名称: ATP grasp ligase (2 entities in total)
• 機能のキーワード: ripp, macrocyclase, ligase
• 由来する生物種: Microcystis aeruginosa MRC
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 76053.98

構造登録者

Li, K.,Condurso, H.L.,Bruner, S.D. (登録日: 2016-02-27, 公開日: 2016-09-21, 最終更新日: 2024-10-23)

主引用文献

Li, K.,Condurso, H.L.,Li, G.,Ding, Y.,Bruner, S.D.
Structural basis for precursor protein-directed ribosomal peptide macrocyclization.
Nat.Chem.Biol., 12:973-979, 2016

PubMed Abstract: Macrocyclization is a common feature of natural product biosynthetic pathways including the diverse family of ribosomal peptides. Microviridins are architecturally complex cyanobacterial ribosomal peptides that target proteases with potent reversible inhibition. The product structure is constructed via three macrocyclizations catalyzed sequentially by two members of the ATP-grasp family, a unique strategy for ribosomal peptide macrocyclization. Here we describe in detail the structural basis for the enzyme-catalyzed macrocyclizations in the microviridin J pathway of Microcystis aeruginosa. The macrocyclases MdnC and MdnB interact with a conserved α-helix of the precursor peptide using a novel precursor-peptide recognition mechanism. The results provide insight into the unique protein-protein interactions that are key to the chemistry, suggest an origin for the natural combinatorial synthesis of microviridin peptides, and provide a framework for future engineering efforts to generate designed compounds.

PubMed: 27669417
DOI: 10.1038/nchembio.2200

実験手法

X-RAY DIFFRACTION (2.278 Å)