The tetramer structure of the glycoside hydrolase family 27 alpha-galactosidase I from Umbelopsis vinacea.
The crystal structure of Umbelopsis vinacea alpha-galactosidase I, which belongs to glycoside hydrolase family 27, was determined at 2.0 A resolution. The monomer structure was well conserved with those of glycoside hydrolase family 27 enzymes. The biological tetramer structure of this enzyme was constructed by the crystallographic 4-fold symmetry, and tetramerization appeared to be caused by three inserted peptides that were involved in the tetramer interface. The quaternary structure indicated that the substrate specificity of this enzyme might be related to the tetramer formation. Three N-glycosylated sugar chains were observed, and their structures were found to be of the high-mannose type.
Fujimoto
Zui
Z
Protein Research Unit, National Institute of Agrobiological Sciences, Tsukuba, Ibaraki, Japan. zui@affrc.go.jp
Kaneko
Satoshi
S
Kim
Wook-Dong
WD
Park
Gwi-Gun
GG
Momma
Mitsuru
M
Kobayashi
Hideyuki
H
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009090:Mucorales / Q000201:enzymology*; D055503:Protein Multimerization; D020836:Protein Structure, Quaternary; D016415:Sequence Alignment; D000519:alpha-Galactosidase / Q000737:chemistry* / Q000378:metabolism
D001426:Bacterial Proteins; C115462:alpha-galactosidase I; D000519:alpha-Galactosidase