7ULF

l-glutamate/GTP complex of F420-gamma glutamyl ligase (CofE) from Archaeoglobus fulgidus

7ULF の概要

• エントリーDOI: 10.2210/pdb7ulf/pdb
• 関連するPDBエントリー: 7ULD 7ULE
• 分子名称: Coenzyme F420:L-glutamate ligase, GAMMA-L-GLUTAMIC ACID, GUANOSINE-5'-TRIPHOSPHATE, ... (5 entities in total)
• 機能のキーワード: ligase substrate complex, ligase
• 由来する生物種: Archaeoglobus fulgidus DSM 4304
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 28203.75

構造登録者

Bashiri, G.,Squire, C.J. (登録日: 2022-04-04, 公開日: 2023-04-12, 最終更新日: 2024-10-23)

主引用文献

Bashiri, G.,Bulloch, E.M.M.,Bramley, W.R.,Davidson, M.,Stuteley, S.M.,Young, P.G.,Harris, P.W.R.,Naqvi, M.S.H.,Middleditch, M.J.,Schmitz, M.,Chang, W.C.,Baker, E.N.,Squire, C.J.
Poly-gamma-glutamylation of biomolecules.
Nat Commun, 15:1310-1310, 2024

PubMed Abstract: Poly-γ-glutamate tails are a distinctive feature of archaeal, bacterial, and eukaryotic cofactors, including the folates and F. Despite decades of research, key mechanistic questions remain as to how enzymes successively add glutamates to poly-γ-glutamate chains while maintaining cofactor specificity. Here, we show how poly-γ-glutamylation of folate and F by folylpolyglutamate synthases and γ-glutamyl ligases, non-homologous enzymes, occurs via processive addition of L-glutamate onto growing γ-glutamyl chain termini. We further reveal structural snapshots of the archaeal γ-glutamyl ligase (CofE) in action, crucially including a bulged-chain product that shows how the cofactor is retained while successive glutamates are added to the chain terminus. This bulging substrate model of processive poly-γ-glutamylation by terminal extension is arguably ubiquitous in such biopolymerisation reactions, including addition to folates, and demonstrates convergent evolution in diverse species from archaea to humans.

PubMed: 38346985
DOI: 10.1038/s41467-024-45632-1

実験手法

X-RAY DIFFRACTION (1.61 Å)