Crystallization and preliminary X-ray crystallographic analysis of the alpha-2,6-sialyltransferase PM0188 from Pasteurella multosida.
Sialyltransferase is an enzyme that transfers the sialic acid moiety from cytidine-5-monophospho-N-acetylneuraminic acid (CMP-NeuAc) to the carbohydrate group of various glycoproteins. These glycoproteins are involved in inflammation, embryogenesis, immune defence and metastasis of cancer cells by cell-cell interactions or cell-matrix interactions. The alpha-2,6-sialyltransferase PM0188 from Pasteurella multocida was purified using affinity-column chromatographic methods and crystallized using the hanging-drop vapour-diffusion method at 293 K. MAD data were collected to 1.9 A resolution from an SeMet-substituted crystal. The crystal belongs to space group P2(1), with unit-cell parameters a = 52.9, b = 61.0, c = 64.6 A, alpha = gamma = 90, beta = 112.3 degrees. Assuming the presence of one molecule in the asymmetric unit, the solvent content is estimated to be about 45%.
Kim
Dong-Uk
DU
Department of Biology, Yonsei University, Seoul 120-749, South Korea.
Yoo
Ji-Ho
JH
Ryu
Kang
K
Cho
Hyun-Soo
HS
D001426:Bacterial Proteins / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000302:isolation & purification; D002846:Chromatography, Affinity; D003460:Crystallization; D018360:Crystallography, X-Ray; D003569:Cytidine Monophosphate N-Acetylneuraminic Acid / Q000737:chemistry / Q000378:metabolism; D016979:Pasteurella multocida / Q000201:enzymology*; D011994:Recombinant Proteins / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000302:isolation & purification; D012799:Sialyltransferases / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000302:isolation & purification; D012997:Solvents; D000094802:beta-D-Galactoside alpha 2-6-Sialyltransferase
D001426:Bacterial Proteins; D011994:Recombinant Proteins; D012997:Solvents; D003569:Cytidine Monophosphate N-Acetylneuraminic Acid; D012799:Sialyltransferases; D000094802:beta-D-Galactoside alpha 2-6-Sialyltransferase