7ULD

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

Summary for 7ULD

• Entry DOI: 10.2210/pdb7uld/pdb
• Related: 6vw3 6vw5
• Descriptor: Coenzyme F420:L-glutamate ligase, CARBONATE ION, MANGANESE (II) ION, ... (7 entities in total)
• Functional Keywords: ligase substrate complex, ligase
• Biological source: Archaeoglobus fulgidus DSM 4304
• Total number of polymer chains: 1
• Total formula weight: 28427.81

Authors

Bashiri, G.,Squire, C.J. (deposition date: 2022-04-04, release date: 2023-04-12, Last modification date: 2024-10-23)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.3 Å)