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

Shanteri Singh, Youngchang Kim, Fengbin Wang, Lance Bigelow, Michael Endres, Madan K. Kharel, Gyorgy Babnigg, Craig A. Bingman, Andrzej Joachimiak, Jon S. Thorson, George N. Phillips

Research output: Contribution to journalArticlepeer-review

9 Scopus citations

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.

Original languageEnglish
Pages (from-to)1547-1554
Number of pages8
JournalProteins: Structure, Function and Bioinformatics
Volume83
Issue number8
DOIs
StatePublished - Aug 1 2015

Bibliographical note

Publisher Copyright:
© 2015 Wiley Periodicals, Inc.

Keywords

  • Carbohydrate
  • Indolocarbazole
  • Natural product
  • Sugar nucleotide
  • Transamination
  • X-ray crystallography

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Molecular Biology

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