1U8X

CRYSTAL STRUCTURE OF GLVA FROM BACILLUS SUBTILIS, A METAL-REQUIRING, NAD-DEPENDENT 6-PHOSPHO-ALPHA-GLUCOSIDASE

「1NRH」から置き換えられました

1U8X の概要

• エントリーDOI: 10.2210/pdb1u8x/pdb
• 関連するPDBエントリー: 1NRH
• 分子名称: Maltose-6'-phosphate glucosidase, 6-O-phosphono-alpha-D-glucopyranose, MANGANESE (II) ION, ... (5 entities in total)
• 機能のキーワード: structural genomics, psi, protein structure initiative, mcsg, glucosidase, nad-dependent, midwest center for structural genomics, hydrolase
• 由来する生物種: Bacillus subtilis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 55062.83

構造登録者

Rajan, S.S.,Yang, X.,Collart, F.,Anderson, W.F.,Midwest Center for Structural Genomics (MCSG) (登録日: 2004-08-09, 公開日: 2004-08-24, 最終更新日: 2024-11-20)

主引用文献

Rajan, S.S.,Yang, X.,Collart, F.,Yip, V.L.,Withers, S.G.,Varrot, A.,Thompson, J.,Davies, G.J.,Anderson, W.F.
Novel Catalytic Mechanism of Glycoside Hydrolysis Based on the Structure of an NAD(+)/Mn(2+)-Dependent Phospho-alpha-Glucosidase from Bacillus subtilis.
STRUCTURE, 12:1619-1629, 2004

PubMed Abstract: GlvA, a 6-phospho-alpha-glucosidase from Bacillus subtilis, catalyzes the hydrolysis of maltose-6'-phosphate and belongs to glycoside hydrolase family GH4. GH4 enzymes are unique in their requirement for NAD(H) and a divalent metal for activity. We have determined the crystal structure of GlvA in complex with its ligands to 2.05 A resolution. Analyses of the active site architecture, in conjunction with mechanistic studies and precedent from the nucleotide diphosphate hexose dehydratases and other systems, suggest a novel mechanism of glycoside hydrolysis by GlvA that involves both the NAD(H) and the metal.

PubMed: 15341727
DOI: 10.1016/j.str.2004.06.020

実験手法

X-RAY DIFFRACTION (2.05 Å)