Crystal structure of α/β-galactoside α2,3-sialyltransferase from a luminous marine bacterium, Photobacterium phosphoreum

Toru Iwatani, Nozomu Okino, Mai Sakakura, Hitomi Kajiwara, Yoshimitsu Takakura, Makoto Kimura, Makoto Ito, Takeshi Yamamoto, Yoshimitsu Kakuta

研究成果: ジャーナルへの寄稿学術誌査読

25 被引用数 (Scopus)

抄録

α/β-Galactoside α2,3-sialyltransferase produced by Photobacterium phosphoreum JT-ISH-467 is a unique enzyme that catalyzes the transfer of N-acetylneuraminic acid residue from cytidine monophosphate N-acetylneuraminic acid to acceptor carbohydrate groups. The enzyme recognizes both mono- and di-saccharides as acceptor substrates, and can transfer Neu5Ac to both α-galactoside and β-galactoside, efficiently. To elucidate the structural basis for the broad acceptor substrate specificity, we determined the crystal structure of the α2,3-sialyltransferase in complex with CMP. The overall structure belongs to the glycosyltransferase-B structural group. We could model a reasonable active conformation structure based on the crystal structure. The predicted structure suggested that the broad substrate specificity could be attributed to the wider entrance of the acceptor substrate binding site.

本文言語英語
ページ(範囲)2083-2087
ページ数5
ジャーナルFEBS Letters
583
12
DOI
出版ステータス出版済み - 6月 18 2009

!!!All Science Journal Classification (ASJC) codes

  • 生物理学
  • 構造生物学
  • 生化学
  • 分子生物学
  • 遺伝学
  • 細胞生物学

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