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Structural characterization of AtmS13, a putative sugar aminotransferase involved in indolocarbazole AT 2433 aminopentose biosynthesis
Author(s) -
Singh Shanteri,
Kim Youngchang,
Wang Fengbin,
Bigelow Lance,
Endres Michael,
Kharel Madan K.,
Babnigg Gyorgy,
Bingman Craig A.,
Joachimiak Andrzej,
Thorson Jon S.,
Phillips George N.
Publication year - 2015
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.24844
Subject(s) - biochemistry , sugar , biosynthesis , chemistry , pentose , stereochemistry , hexose , enzyme , nucleotide , gene , fermentation
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. Proteins 2015; 83:1547–1554. © 2015 Wiley Periodicals, Inc.