9TGV

Guanidine prenyltransferase NosH apo structure

Summary for 9TGV

• Entry DOI: 10.2210/pdb9tgv/pdb
• Descriptor: NosH, GLYCEROL (3 entities in total)
• Functional Keywords: nosh facilitates the magnesium-dependent transfer of guanidine groups to polyprenyl diphosphates of differing chain lengths, alongside the hydrolysis of the diphosphate moiety, transferase
• Biological source: Nostoc flagelliforme CCNUN1
• Total number of polymer chains: 1
• Total formula weight: 29820.10

Authors

Kolling, D.,Koehnke, J. (deposition date: 2025-12-02, release date: 2026-11-04)

Primary citation

Kolling, D.,Konzok, K.,Taser, D.,Jentsch, T.,Schwoerer, S.,Struwe, H.,Bultemeier, A.,Freiberg, J.,Witte, C.P.,Franke, J.,Luzhetskyy, A.,Kirschning, A.,Rudorf, S.,Koehnke, J.
Natural product biosynthesis by guanidine prenyltransferases in plants and bacteria.
Science, 394:413-418, 2026

PubMed Abstract: Guanidine exists almost exclusively as a resonance-stabilized cation, making its direct enzymatic functionalization challenging. We identified the cyanobacterial enzyme NosH, which catalyzes direct prenyl transfer to free guanidine. Structural and mechanistic analyses revealed guanidine activation by a two-aspartate clamp coupled to prenyl-donor binding through a distinct catalytic architecture. Guided by these features, we identified a large family of guanidine prenyltransferases across bacteria and plants. Plant enzymes produced guanidine alkaloids such as galegine in vitro and heterologous expression of a plant ortholog in produced galegine in planta, providing a direct enzymatic link to plant-specialized metabolism.

PubMed: 42912132
DOI: 10.1126/science.aeg1821

Experimental method

X-RAY DIFFRACTION (1.35 Å)