7FC0

Reconstitution of MbnABC complex from Rugamonas rubra ATCC-43154 (GroupIII)

7FC0 の概要

• エントリーDOI: 10.2210/pdb7fc0/pdb
• 分子名称: RrMbnA precosur peptide, Methanobactin biosynthesis cassette protein MbnB, Methanobactin biosynthesis cassette protein MbnC, ... (6 entities in total)
• 機能のキーワード: fe binding protein, mbnabc complex, methanobactin., metal binding protein
• 由来する生物種: Rugamonas rubra; 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 109686.04

構造登録者

Chao, D.,Zhaolin, L.,Shoujie, L.,Li, Z.,Dan, Z.,Ying, J.,Wei, C. (登録日: 2021-07-13, 公開日: 2022-03-16, 最終更新日: 2023-11-29)

主引用文献

Dou, C.,Long, Z.,Li, S.,Zhou, D.,Jin, Y.,Zhang, L.,Zhang, X.,Zheng, Y.,Li, L.,Zhu, X.,Liu, Z.,He, S.,Yan, W.,Yang, L.,Xiong, J.,Fu, X.,Qi, S.,Ren, H.,Chen, S.,Dai, L.,Wang, B.,Cheng, W.
Crystal structure and catalytic mechanism of the MbnBC holoenzyme required for methanobactin biosynthesis.
Cell Res., 32:302-314, 2022

PubMed Abstract: Methanobactins (Mbns) are a family of copper-binding peptides involved in copper uptake by methanotrophs, and are potential therapeutic agents for treating diseases characterized by disordered copper accumulation. Mbns are produced via modification of MbnA precursor peptides at cysteine residues catalyzed by the core biosynthetic machinery containing MbnB, an iron-dependent enzyme, and MbnC. However, mechanistic details underlying the catalysis of the MbnBC holoenzyme remain unclear. Here, we present crystal structures of MbnABC complexes from two distinct species, revealing that the leader peptide of the substrate MbnA binds MbnC for recruitment of the MbnBC holoenzyme, while the core peptide of MbnA resides in the catalytic cavity created by the MbnB-MbnC interaction which harbors a unique tri-iron cluster. Ligation of the substrate sulfhydryl group to the tri-iron center achieves a dioxygen-dependent reaction for oxazolone-thioamide installation. Structural analysis of the MbnABC complexes together with functional investigation of MbnB variants identified a conserved catalytic aspartate residue as a general base required for MbnBC-mediated MbnA modification. Together, our study reveals the similar architecture and function of MbnBC complexes from different species, demonstrating an evolutionarily conserved catalytic mechanism of the MbnBC holoenzymes.

PubMed: 35110668
DOI: 10.1038/s41422-022-00620-2

実験手法

X-RAY DIFFRACTION (2.643 Å)