5T4A

Crystal structure of BhGH81 in complex with laminaro-hexaose

5T4A の概要

• エントリーDOI: 10.2210/pdb5t4a/pdb
• 関連するPDBエントリー: 5T49 5T4C 5T4G
• 分子名称: Glycoside Hydrolase, beta-D-glucopyranose-(1-3)-alpha-D-glucopyranose, beta-D-glucopyranose-(1-3)-beta-D-glucopyranose-(1-3)-beta-D-glucopyranose, ... (6 entities in total)
• 機能のキーワード: (alpha/beta)6 barrel, glycoside hydrolase, hydrolase
• 由来する生物種: Bacillus halodurans
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 89792.76

構造登録者

Pluvinage, B.,Boraston, A.B. (登録日: 2016-08-29, 公開日: 2017-06-28, 最終更新日: 2023-10-04)

主引用文献

Pluvinage, B.,Fillo, A.,Massel, P.,Boraston, A.B.
Structural Analysis of a Family 81 Glycoside Hydrolase Implicates Its Recognition of beta-1,3-Glucan Quaternary Structure.
Structure, 25:1348-1359.e3, 2017

PubMed Abstract: Family 81 glycoside hydrolases (GHs), which are known to cleave β-1,3-glucans, are found in archaea, bacteria, eukaryotes, and viruses. Here we examine the structural and functional features of the GH81 catalytic module, BhGH81, from the Bacillus halodurans protein BH0236 to probe the molecular basis of β-1,3-glucan recognition and cleavage. BhGH81 displayed activity on laminarin, curdlan, and pachyman, but not scleroglucan; the enzyme also cleaved β-1,3-glucooligosaccharides as small as β-1,3-glucotriose. The crystal structures of BhGH81 in complex with various β-1,3-glucooligosaccharides revealed distorted sugars in the -1 catalytic subsite and an arrangement consistent with an inverting catalytic mechanism having a proposed conformational itinerary of S → B → S. Notably, the architecture of the catalytic site, location of an adjacent ancillary β-1,3-glucan binding site, and the surface properties of the enzyme indicate the likely ability to recognize the double and/or triple-helical quaternary structures adopted by β-1,3-glucans.

PubMed: 28781080
DOI: 10.1016/j.str.2017.06.019

実験手法

X-RAY DIFFRACTION (2.1 Å)