7M4S

Crystal structure of macrocyclase AMdnB from Anabaena sp. PCC 7120

7M4S の概要

• エントリーDOI: 10.2210/pdb7m4s/pdb
• 分子名称: AMdnB protein (2 entities in total)
• 機能のキーワード: natural products, ripps, macrocyclase, biosynthetic protein
• 由来する生物種: Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 165142.17

構造登録者

Li, G.,Bruner, S.D. (登録日: 2021-03-22, 公開日: 2021-11-03, 最終更新日: 2024-10-23)

主引用文献

Li, G.,Patel, K.,Zhang, Y.,Pugmire, J.K.,Ding, Y.,Bruner, S.D.
Structural and biochemical studies of an iterative ribosomal peptide macrocyclase.
Proteins, 90:670-679, 2022

PubMed Abstract: Microviridins, tricyclic peptide natural products originally isolated from cyanobacteria, function as inhibitors of diverse serine-type proteases. Here we report the structure and biochemical characterization of AMdnB, a unique iterative macrocyclase involved in a microviridin biosynthetic pathway from Anabaena sp. PCC 7120. The ATP-dependent cyclase, along with the homologous AMdnC, introduce up to nine macrocyclizations on three distinct core regions of a precursor peptide, AMdnA. The results presented here provide structural and mechanistic insight into the iterative chemistry of AMdnB. In vitro AMdnB-catalyzed cyclization reactions demonstrate the synthesis of the two predicted tricyclic products from a multi-core precursor peptide substrate, consistent with a distributive mode of catalysis. The X-ray structure of AMdnB shows a structural motif common to ATP-grasp cyclases involved in RiPPs biosynthesis. Additionally, comparison with the noniterative MdnB allows insight into the structural basis for the iterative chemistry. Overall, the presented results provide insight into the general mechanism of iterative enzymes in ribosomally synthesized and post-translationally modified peptide biosynthetic pathways.

PubMed: 34664307
DOI: 10.1002/prot.26264

実験手法

X-RAY DIFFRACTION (2.493 Å)