Journal
BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY
Volume 73, Issue 10, Pages 2360-2364Publisher
TAYLOR & FRANCIS LTD
DOI: 10.1271/bbb.90604
Keywords
crystal structure; alpha-galactosidase; glycoprotein; Umbelopsis vinacea; tetramer
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Funding
- Japan Society for the Promotion of Science
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The crystal structure of Umbelopsis vinacea alpha-galactosidase 1, which belongs to glycoside hydrolase family 27, was determined at 2.0 angstrom 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.
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