6BWH

Crystal structure of Mycoibacterium tuberculosis Rv2983 in complex with PEP

6BWH の概要

• エントリーDOI: 10.2210/pdb6bwh/pdb
• 分子名称: 2-phospho-L-lactate guanylyltransferase, PHOSPHOENOLPYRUVATE, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: alpha/beta structure, transferase
• 由来する生物種: Mycobacterium tuberculosis
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 71219.09

構造登録者

Bashiri, G.,Jirgis, E.N.M.,Baker, E.N. (登録日: 2017-12-15, 公開日: 2018-12-19, 最終更新日: 2023-11-15)

主引用文献

Bashiri, G.,Antoney, J.,Jirgis, E.N.M.,Shah, M.V.,Ney, B.,Copp, J.,Stuteley, S.M.,Sreebhavan, S.,Palmer, B.,Middleditch, M.,Tokuriki, N.,Greening, C.,Scott, C.,Baker, E.N.,Jackson, C.J.
A revised biosynthetic pathway for the cofactor F420in prokaryotes.
Nat Commun, 10:1558-1558, 2019

PubMed Abstract: Cofactor F plays critical roles in primary and secondary metabolism in a range of bacteria and archaea as a low-potential hydride transfer agent. It mediates a variety of important redox transformations involved in bacterial persistence, antibiotic biosynthesis, pro-drug activation and methanogenesis. However, the biosynthetic pathway for F has not been fully elucidated: neither the enzyme that generates the putative intermediate 2-phospho-L-lactate, nor the function of the FMN-binding C-terminal domain of the γ-glutamyl ligase (FbiB) in bacteria are known. Here we present the structure of the guanylyltransferase FbiD and show that, along with its archaeal homolog CofC, it accepts phosphoenolpyruvate, rather than 2-phospho-L-lactate, as the substrate, leading to the formation of the previously uncharacterized intermediate dehydro-F-0. The C-terminal domain of FbiB then utilizes FMNH to reduce dehydro-F-0, which produces mature F species when combined with the γ-glutamyl ligase activity of the N-terminal domain. These new insights have allowed the heterologous production of F from a recombinant F biosynthetic pathway in Escherichia coli.

PubMed: 30952857
DOI: 10.1038/s41467-019-09534-x

実験手法

X-RAY DIFFRACTION (2.18 Å)