3A5V

Crystal structure of alpha-galactosidase I from Mortierella vinacea

3A5V の概要

• エントリーDOI: 10.2210/pdb3a5v/pdb
• 分子名称: Alpha-galactosidase, alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (7 entities in total)
• 機能のキーワード: beta/alpha barrel, n-glycosylation, hydrolase
• 由来する生物種: Umbelopsis vinacea
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 47322.66

構造登録者

Fujimoto, Z.,Kaneko, S.,Kobayashi, H. (登録日: 2009-08-12, 公開日: 2009-08-25, 最終更新日: 2024-11-20)

主引用文献

Fujimoto, Z.,Kaneko, S.,Kim, W.-D.,Park, G.-G.,Momma, M.,Kobayashi, H.
The Tetramer Structure of the Glycoside Hydrolase Family 27 alpha-Galactosidase I from Umbelopsis vinacea
Biosci.Biotechnol.Biochem., 73:2360-2364, 2009

PubMed Abstract: 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.

PubMed: 19809163
DOI: 10.1271/bbb.90604

実験手法

X-RAY DIFFRACTION (2 Å)