2BHY

Crystal structure of Deinococcus radiodurans maltooligosyltrehalose trehalohydrolase in complex with trehalose

2BHY の概要

• エントリーDOI: 10.2210/pdb2bhy/pdb
• 関連するPDBエントリー: 2BHU 2BHZ
• 関連するBIRD辞書のPRD_ID: PRD_900006
• 分子名称: MALTOOLIGOSYLTREHALOSE TREHALOHYDROLASE, alpha-D-glucopyranose-(1-1)-alpha-D-glucopyranose, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ... (7 entities in total)
• 機能のキーワード: hydrolase, d. radiodurans, trehalose, alpha-amylase, protein- carbohydrate complex, desiccation resistance, glycosidase
• 由来する生物種: DEINOCOCCUS RADIODURANS
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 70726.89

構造登録者

Timmins, J.,Leiros, H.-K.S.,Leonard, G.,Leiros, I.,McSweeney, S. (登録日: 2005-01-20, 公開日: 2005-03-31, 最終更新日: 2020-07-29)

主引用文献

Timmins, J.,Leiros, H.-K.S.,Leonard, G.,Leiros, I.,Mcsweeney, S.
Crystal Structure of Maltooligosyltrehalose Trehalohydrolase from Deinococcus Radiodurans in Complex with Disaccharides
J.Mol.Biol., 347:949-, 2005

PubMed Abstract: Trehalose (alpha-D-glucopyranosyl-1,1-alpha-D-glucopyranose) is a non-reducing diglucoside found in various organisms that serves as a carbohydrate reserve and as an agent that protects against a variety of physical and chemical stresses. Deinococcus radiodurans possesses an alternative biosynthesis pathway for the synthesis of trehalose from maltooligosaccharides. This reaction is mediated by two enzymes: maltooligosyltrehalose synthase (MTSase) and maltooligosyltrehalose trehalohydrolase (MTHase). Here, we present the 1.1A resolution crystal structure of MTHase. It consists of three major domains: two beta-sheet domains and a conserved glycosidase (beta/alpha)8 barrel catalytic domain. Three subdomains consisting of short insertions were identified within the catalytic domain. Subsequently, structures of MTHase in complex with maltose and trehalose were obtained at 1.2 A and 1.5 A resolution, respectively. These structures reveal the importance of the three inserted subdomains in providing the key residues required for substrate recognition. Trehalose is recognised specifically in the +1 and +2 binding subsites by an extensive hydrogen-bonding network and a strong hydrophobic stacking interaction in between two aromatic residues. Moreover, upon binding to maltose, which mimics the substrate sugar chain, a major concerted conformational change traps the sugar chain in the active site. The presence of magnesium in the active site of the MTHase-maltose complex suggests that MTHase activity may be regulated by divalent cations.

PubMed: 15784255
DOI: 10.1016/J.JMB.2005.02.011

実験手法

X-RAY DIFFRACTION (1.5 Å)