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Proteins. 2015 Aug;83(8):1547-54. doi: 10.1002/prot.24844. Epub 2015 Jul 1.

Structural characterization of AtmS13, a putative sugar aminotransferase involved in indolocarbazole AT2433 aminopentose biosynthesis.

Author information

1
Center for Pharmaceutical Research and Innovation, Pharmaceutical Sciences Division, University of Kentucky College of Pharmacy, Lexington, Kentucky, 40536-0596.
2
Midwest Center for Structural Genomics and Structural Biology Center, Biosciences Division, Argonne National Laboratory, Argonne, Illinois, 60439.
3
Department of BioSciences, Rice University, Houston, Texas, 77005.
4
School of Pharmacy, Department of Pharmaceutical Sciences, University of Maryland Eastern Shore, Princess Anne, Maryland.
5
Department of Biochemistry, University of Wisconsin-Madison, Madison, Wisconsin, 53706.
6
Department of Chemistry, Rice University, Houston, Texas, 77005.

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.

KEYWORDS:

X-ray crystallography; carbohydrate; indolocarbazole; natural product; sugar nucleotide; transamination

PMID:
26061967
PMCID:
PMC4570032
DOI:
10.1002/prot.24844
[Indexed for MEDLINE]
Free PMC Article

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