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.
| 元の言語 | 英語 |
|---|---|
| ページ（範囲） | 2083-2087 |
| ページ数 | 5 |
| ジャーナル | FEBS Letters |
| 巻 | 583 |
| 発行部数 | 12 |
| DOI | |
| 出版物ステータス | 出版済み - 6 18 2009 |
Fingerprint
All Science Journal Classification (ASJC) codes
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology
これを引用
Crystal structure of α/β-galactoside α2,3-sialyltransferase from a luminous marine bacterium, Photobacterium phosphoreum. / Iwatani, Toru; Okino, Nozomu; Sakakura, Mai; Kajiwara, Hitomi; Takakura, Yoshimitsu; Kimura, Makoto; Ito, Makoto; Yamamoto, Takeshi; Kakuta, Yoshimitsu.
：: FEBS Letters, 巻 583, 番号 12, 18.06.2009, p. 2083-2087.研究成果: ジャーナルへの寄稿 › 記事
}
TY - JOUR
T1 - Crystal structure of α/β-galactoside α2,3-sialyltransferase from a luminous marine bacterium, Photobacterium phosphoreum
AU - Iwatani, Toru
AU - Okino, Nozomu
AU - Sakakura, Mai
AU - Kajiwara, Hitomi
AU - Takakura, Yoshimitsu
AU - Kimura, Makoto
AU - Ito, Makoto
AU - Yamamoto, Takeshi
AU - Kakuta, Yoshimitsu
PY - 2009/6/18
Y1 - 2009/6/18
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=67349084731&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=67349084731&partnerID=8YFLogxK
U2 - 10.1016/j.febslet.2009.05.032
DO - 10.1016/j.febslet.2009.05.032
M3 - Article
VL - 583
SP - 2083
EP - 2087
JO - FEBS Letters
JF - FEBS Letters
SN - 0014-5793
IS - 12
ER -