9US4

Klebsiella pneumoniae maltohexaose-producing alpha-amylase in complex with acarbose

9US4 の概要

• エントリーDOI: 10.2210/pdb9us4/pdb
• 関連するBIRD辞書のPRD_ID: PRD_900007 PRD_900022 PRD_900110
• 分子名称: Maltohexaose-producing amylase, 4,6-dideoxy-4-{[(1S,4R,5S,6S)-4,5,6-trihydroxy-3-(hydroxymethyl)cyclohex-2-en-1-yl]amino}-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-beta-D-glucopyranose, 4,6-dideoxy-4-{[(1S,4R,5S,6S)-4,5,6-trihydroxy-3-(hydroxymethyl)cyclohex-2-en-1-yl]amino}-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, ... (6 entities in total)
• 機能のキーワード: glycosyl hydrolase family 13, hydrolase
• 由来する生物種: Klebsiella pneumoniae
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 153059.27

構造登録者

Fujimoto, Z.,Kishine, N.,Momma, M. (登録日: 2025-05-01, 公開日: 2025-07-09, 最終更新日: 2025-09-03)

主引用文献

Fujimoto, Z.,Kishine, N.,Momma, M.
Crystal structure of Klebsiella pneumoniae maltohexaose-producing alpha-amylase.
J.Biochem., 178:201-207, 2025

PubMed Abstract: The α-amylase from Klebsiella pneumoniae (KpAmy13), which belongs to glycoside hydrolase family 13 subfamily 19, produces maltohexaose as an initial product when acting on starch and has been characterized as a maltohexaose-producing α-amylase. The crystal structure of KpAmy13 was determined at a resolution of 1.9 Å, revealing the structures of all its domains: N, A, B and C. Domain N resembles the starch-binding domain known as carbohydrate-binding module family 69, found in α-glucan-related proteins. Although domain N does not conserve the starch-binding residues observed in other proteins, it has several hydrophobic residues on its surface, which might be involved in promoting catalysis. The catalytic cleft is located at the bottom of a circular depression. The domain N-truncated mutant of KpAmy13 in complex with maltohexaose showed that its non-reducing end glucose docks at subsite -6. The long and complex structure of domain B contributes to forming a cleft of the right size for six glucose moieties, demonstrating the exo-acting mechanism.

PubMed: 40576559
DOI: 10.1093/jb/mvaf034

実験手法

X-RAY DIFFRACTION (1.95 Å)