9x86

Crystal Structure of dehydratase ApmL in Amipurimycin biosynthesis

spinqualitylabelsall models 9x86, resolution 3.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9x86 is a 1 chain structure with sequence from Streptomyces. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.5Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Amipurimycin is a peptidyl nucleoside antibiotic characterized by a C(9) 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. Deoxysugar Formation via 4',5'-Dehydration on PKS Assembly Line in Nucleoside Antibiotic Biosynthesis.,Chen ZH, Wang F, Wang W, Zhang TC, Wang YL, Zhang WH, Pu J, Sun A, Pan HX, Tang GL Angew Chem Int Ed Engl. 2026 Mar 28:e6927983. doi: 10.1002/anie.6927983. PMID:41902592 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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