31KA
Guanidine prenyltransferase mutant NosHRP in complex L-arginine
Summary for 31KA
| Entry DOI | 10.2210/pdb31ka/pdb |
| Descriptor | Guanidine transferase, GLYCEROL, ACETATE ION, ... (7 entities in total) |
| Functional Keywords | noshrp facilitates the magnesium-dependent transfer of l-arginine 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 | 2 |
| Total formula weight | 60640.26 |
| Authors | |
| 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 Cited by 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: 42912132DOI: 10.1126/science.aeg1821 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.85 Å) |
Structure validation
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