2zwi | pdb_00002zwi

Crystal structure of alpha/beta-Galactoside alpha-2,3-Sialyltransferase from a Luminous Marine Bacterium, Photobacterium phosphoreum

spinqualitylabelsall models 2zwi, resolution 2.01Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2zwi is a 2 chain structure with sequence from "acinetobacter_phosphorescens"_brisou_1955 "acinetobacter phosphorescens" brisou 1955. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: C5P, CL, GOL, ZN Gene: pst3-467 ("Acinetobacter phosphorescens" Brisou 1955) Activity: Beta-galactoside alpha-2,3-sialyltransferase, with EC number 2.4.99.4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. Crystal structure of alpha/beta-galactoside alpha2,3-sialyltransferase from a luminous marine bacterium, Photobacterium phosphoreum.,Iwatani T, Okino N, Sakakura M, Kajiwara H, Takakura Y, Kimura M, Ito M, Yamamoto T, Kakuta Y FEBS Lett. 2009 Jun 18;583(12):2083-7. Epub 2009 May 23. PMID:19467231 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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