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

Research output: Contribution to journalArticlepeer-review

24 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)2083-2087
Number of pages5
JournalFEBS Letters
Volume583
Issue number12
DOIs
Publication statusPublished - Jun 18 2009

All Science Journal Classification (ASJC) codes

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

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