3VPS

Structure of a novel NAD dependent-NDP-hexosamine 5,6-dehydratase, TunA, involved in tunicamycin biosynthesis

Summary for 3VPS

• Entry DOI: 10.2210/pdb3vps/pdb
• Descriptor: NAD-dependent epimerase/dehydratase, URIDINE-DIPHOSPHATE-N-ACETYLGLUCOSAMINE, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, ... (4 entities in total)
• Functional Keywords: tunicamycins, biosynthesis, exo-glycal, dehydratase, rossmann fold, transferase
• Biological source: Streptomyces chartreusis
• Total number of polymer chains: 2
• Total formula weight: 72907.21

Authors

Wyszynski, F.J.,Lee, S.S.,Yabe, T.,Wang, H.,Gomez-Escribano, J.P.,Bibb, M.J.,Lee, S.J.,Davies, G.J.,Davis, B.G. (deposition date: 2012-03-12, release date: 2012-04-18, Last modification date: 2024-03-20)

• Primary citation: Wyszynski, F.J.,Lee, S.S.,Yabe, T.,Wang, H.,Gomez-Escribano, J.P.,Bibb, M.J.,Lee, S.J.,Davies, G.J.,Davis, B.G.; Biosynthesis of nucleoside antibiotic tunicamycin proceeds via unique exo-glycal intermediates; To be published,

Experimental method

X-RAY DIFFRACTION (1.9 Å)