title: Crystal structure of alpha/beta-galactoside alpha2,3-sialyltransferase from a luminous marine bacterium, Photobacterium phosphoreum.
abstract: Alpha/beta-galactoside alpha2,3-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 alpha-galactoside and beta-galactoside, efficiently. To elucidate the structural basis for the broad acceptor substrate specificity, we determined the crystal structure of the alpha2,3-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.
authors.affiliation: Laboratory of Structural Biology, Graduate School of Systems Life Sciences, Kyushu University, Fukuoka 812-8581, Japan.
authors.forename: Toru
authors.initials: T
authors.lastname: Iwatani
authors.forename: Nozomu
authors.initials: N
authors.lastname: Okino
authors.forename: Mai
authors.initials: M
authors.lastname: Sakakura
authors.forename: Hitomi
authors.initials: H
authors.lastname: Kajiwara
authors.forename: Yoshimitsu
authors.initials: Y
authors.lastname: Takakura
authors.forename: Makoto
authors.initials: M
authors.lastname: Kimura
authors.forename: Makoto
authors.initials: M
authors.lastname: Ito
authors.forename: Takeshi
authors.initials: T
authors.lastname: Yamamoto
authors.forename: Yoshimitsu
authors.initials: Y
authors.lastname: Kakuta
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D020134:Catalytic Domain; D018360:Crystallography, X-Ray; D003568:Cytidine Monophosphate / Q000378:metabolism; D003569:Cytidine Monophosphate N-Acetylneuraminic Acid / Q000378:metabolism; D005697:Galactosides / Q000378:metabolism; D008958:Models, Molecular; D010776:Photobacterium / Q000201:enzymology* / Q000235:genetics; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D012799:Sialyltransferases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D055672:Static Electricity; D013379:Substrate Specificity; D000094663:beta-Galactoside alpha-2,3-Sialyltransferase
chemical_list: D001426:Bacterial Proteins; D005697:Galactosides; D011994:Recombinant Proteins; D003569:Cytidine Monophosphate N-Acetylneuraminic Acid; D012799:Sialyltransferases; D003568:Cytidine Monophosphate; D000094663:beta-Galactoside alpha-2,3-Sialyltransferase