4ZWV

Crystal Structure of Aminotransferase AtmS13 from Actinomadura melliaura

Replaces:  4RXK

Summary for 4ZWV

• Entry DOI: 10.2210/pdb4zwv/pdb
• Descriptor: Putative aminotransferase, GLYCEROL (3 entities in total)
• Functional Keywords: aminotransferase, structural genomics, psi-biology, protein structure initiative, enzyme discovery for natural product biosynthesis, natpro, midwest center for structural genomics, mcsg, transferase
• Biological source: Actinomadura melliaura
• Total number of polymer chains: 2
• Total formula weight: 84238.47

Authors

Kim, Y.,Bigelow, L.,Endres, M.,Wang, F.,Phillips Jr., G.N.,Joachimiak, A.,Enzyme Discovery for Natural Product Biosynthesis (NatPro),Midwest Center for Structural Genomics (MCSG) (deposition date: 2015-05-19, release date: 2015-06-03, Last modification date: 2025-04-02)

Primary citation

Singh, S.,Kim, Y.,Wang, F.,Bigelow, L.,Endres, M.,Kharel, M.K.,Babnigg, G.,Bingman, C.A.,Joachimiak, A.,Thorson, J.S.,Phillips, G.N.
Structural characterization of AtmS13, a putative sugar aminotransferase involved in indolocarbazole AT2433 aminopentose biosynthesis.
Proteins, 83:1547-1554, 2015

PubMed Abstract: AT2433 from Actinomadura melliaura is an indolocarbazole antitumor antibiotic structurally distinguished by its unique aminodideoxypentose-containing disaccharide moiety. The corresponding sugar nucleotide-based biosynthetic pathway for this unusual sugar derives from comparative genomics where AtmS13 has been suggested as the contributing sugar aminotransferase (SAT). Determination of the AtmS13 X-ray structure at 1.50-Å resolution reveals it as a member of the aspartate aminotransferase fold type I (AAT-I). Structural comparisons of AtmS13 with homologous SATs that act upon similar substrates implicate potential active site residues that contribute to distinctions in sugar C5 (hexose vs. pentose) and/or sugar C2 (deoxy vs. hydroxyl) substrate specificity.

PubMed: 26061967
DOI: 10.1002/prot.24844

Experimental method

X-RAY DIFFRACTION (1.503 Å)