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: Contribution to journalArticle査読

24 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 18 2009

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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