7ule

F420-1/GDP complex of F420-gamma glutamyl ligase (CofE) from Archaeoglobus fulgidusF420-1/GDP complex of F420-gamma glutamyl ligase (CofE) from Archaeoglobus fulgidus

Structural highlights 7ule is a 1 chain structure with sequence from Archaeoglobus fulgidus DSM 4304. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.7Å Ligands: , , , Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function COFE_ARCFU Catalyzes the GTP-dependent successive addition of two L-glutamates to the L-lactyl phosphodiester of 7,8-didemethyl-8-hydroxy-5-deazariboflavin (F420-0) to form coenzyme F420-0-glutamyl-glutamate (F420-2), with a gamma-linkage between the two glutamates. May be able to add up to four gamma-linked glutamates, since F420-4 is a species that was isolated from A.fulgidus. Publication Abstract from PubMed Poly-gamma-glutamate tails are a distinctive feature of archaeal, bacterial, and eukaryotic cofactors, including the folates and F(420). Despite decades of research, key mechanistic questions remain as to how enzymes successively add glutamates to poly-gamma-glutamate chains while maintaining cofactor specificity. Here, we show how poly-gamma-glutamylation of folate and F(420) by folylpolyglutamate synthases and gamma-glutamyl ligases, non-homologous enzymes, occurs via processive addition of L-glutamate onto growing gamma-glutamyl chain termini. We further reveal structural snapshots of the archaeal gamma-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-gamma-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. Poly-gamma-glutamylation of biomolecules.,Bashiri G, Bulloch EMM, Bramley WR, Davidson M, Stuteley SM, Young PG, Harris PWR, Naqvi MSH, Middleditch MJ, Schmitz M, Chang WC, Baker EN, Squire CJ Nat Commun. 2024 Feb 12;15(1):1310. doi: 10.1038/s41467-024-45632-1. PMID:38346985 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

spinqualitylabelsall models 7ule, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image