9X86

Crystal Structure of dehydratase ApmL in Amipurimycin biosynthesis

Summary for 9X86

• Entry DOI: 10.2210/pdb9x86/pdb
• Descriptor: Amc20 (2 entities in total)
• Functional Keywords: dehydratase, lyase
• Biological source: Streptomyces novoguineensis
• Total number of polymer chains: 1
• Total formula weight: 33292.22

Authors

Wang, W.,Sun, A. (deposition date: 2025-10-18, release date: 2026-04-08)

Primary citation

Chen, Z.H.,Wang, F.,Wang, W.,Zhang, T.C.,Wang, Y.L.,Zhang, W.H.,Pu, J.,Sun, A.,Pan, H.X.,Tang, G.L.
Deoxysugar Formation via 4',5'-Dehydration on PKS Assembly Line in Nucleoside Antibiotic Biosynthesis.
Angew.Chem.Int.Ed.Engl., :e6927983-e6927983, 2026

PubMed Abstract: Amipurimycin is a peptidyl nucleoside antibiotic characterized by a C high-carbon sugar, with potent activity against the rice blast pathogen Pyricularia oryzae. The biosynthetic machinery of the C-4' methylene group in its deoxy sugar has remained unknown. This study reveals that ApmL, a hypothetical protein in the DUF3500 family, functions as a 4',5'-dehydratase whose activity is strictly dependent on the PKS assembly line. Together with its partner reductase ApmM, they complete a two-step C-4' deoxygenation process via dehydration-reduction. We achieve the first in vitro reconstitution of this unique PKS-coupled dehydration process and show direct interaction between ApmL and PKS proteins. Our findings establish ApmL as a new family of dehydratase and uncover a noncanonical deoxygenation strategy in nucleoside antibiotic biosynthesis.

PubMed: 41902592
DOI: 10.1002/anie.6927983

Experimental method

X-RAY DIFFRACTION (3.5 Å)