2OWX

THERMUS THERMOPHILUS AMYLOMALTASE AT pH 5.6

2OWX の概要

• エントリーDOI: 10.2210/pdb2owx/pdb
• 関連するPDBエントリー: 1ESW 1OWC 2OWW
• 分子名称: 4-alpha-glucanotransferase, MALONATE ION, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: beta-alpha-8 barrel, succinimide residue in main chain, transferase
• 由来する生物種: Thermus thermophilus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 57722.38

構造登録者

Barends, T.R.M.,Kaper, T.,Bultema, J.J.,Dijkhuizen, L.,van der Maarel, J.E.C.,Dijkstra, B.W. (登録日: 2007-02-17, 公開日: 2007-04-03, 最終更新日: 2023-11-15)

主引用文献

Barends, T.R.,Bultema, J.B.,Kaper, T.,van der Maarel, M.J.,Dijkhuizen, L.,Dijkstra, B.W.
Three-way stabilization of the covalent intermediate in amylomaltase, an alpha-amylase-like transglycosylase.
J.Biol.Chem., 282:17242-17249, 2007

PubMed Abstract: Amylomaltases are glycosyl hydrolases belonging to glycoside hydrolase family 77 that are capable of the synthesis of large cyclic glucans and the disproportionation of oligosaccharides. Using protein crystallography, we have generated a flip book movie of the amylomaltase catalytic cycle in atomic detail. The structures include a covalent glycosyl enzyme intermediate and a covalent intermediate in complex with an analogue of a co-substrate and show how the structures of both enzyme and substrate respond to the changes required by the catalytic cycle as it proceeds. Notably, the catalytic nucleophile changes conformation dramatically during the reaction. Also, Gln-256 on the 250s loop is involved in orienting the substrate in the +1 site. The absence of a suitable base in the covalent intermediate structure explains the low hydrolysis activity.

PubMed: 17420245
DOI: 10.1074/jbc.M701444200

実験手法

X-RAY DIFFRACTION (2.5 Å)