7ULE
F420-1/GDP complex of F420-gamma glutamyl ligase (CofE) from Archaeoglobus fulgidus
Summary for 7ULE
| Entry DOI | 10.2210/pdb7ule/pdb |
| Related | 7ULD |
| Descriptor | Coenzyme F420:L-glutamate ligase, GUANOSINE-5'-DIPHOSPHATE, (2~{S})-2-[[(2~{S})-2-[oxidanyl-[(2~{R},3~{S},4~{S})-2,3,4-tris(oxidanyl)-5-[2,4,8-tris(oxidanylidene)-1,9-dihydropyrimido[4,5-b]quinolin-10-yl]pentoxy]phosphoryl]oxypropanoyl]amino]pentanedioic acid, ... (6 entities in total) |
| Functional Keywords | ligase substrate complex, ligase |
| Biological source | Archaeoglobus fulgidus DSM 4304 |
| Total number of polymer chains | 1 |
| Total formula weight | 28644.11 |
| 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 Cited by 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: 38346985DOI: 10.1038/s41467-024-45632-1 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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