5U22

Structure of N2152 from Neocallimastix frontalis

5U22 の概要

• エントリーDOI: 10.2210/pdb5u22/pdb
• 分子名称: N2152, 2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, 1,2-ETHANEDIOL, ... (5 entities in total)
• 機能のキーワード: glycoside hydrolase, tim barrel, beta sandwich, hydrolase
• 由来する生物種: Neocallimastix frontalis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 49504.25

構造登録者

Jones, D.R.,Abbott, D.W. (登録日: 2016-11-29, 公開日: 2017-06-14, 最終更新日: 2024-03-06)

主引用文献

Jones, D.R.,Uddin, M.S.,Gruninger, R.J.,Pham, T.T.M.,Thomas, D.,Boraston, A.B.,Briggs, J.,Pluvinage, B.,McAllister, T.A.,Forster, R.J.,Tsang, A.,Selinger, L.B.,Abbott, D.W.
Discovery and characterization of family 39 glycoside hydrolases from rumen anaerobic fungi with polyspecific activity on rare arabinosyl substrates.
J. Biol. Chem., 292:12606-12620, 2017

PubMed Abstract: Enzyme activities that improve digestion of recalcitrant plant cell wall polysaccharides may offer solutions for sustainable industries. To this end, anaerobic fungi in the rumen have been identified as a promising source of novel carbohydrate active enzymes (CAZymes) that modify plant cell wall polysaccharides and other complex glycans. Many CAZymes share insufficient sequence identity to characterized proteins from other microbial ecosystems to infer their function; thus presenting challenges to their identification. In this study, four rumen fungal genes (, , , and ) were identified that encode family 39 glycoside hydrolases (GH39s), and have conserved structural features with GH51s. Two recombinant proteins, NF2152 and NF2523, were characterized using a variety of biochemical and structural techniques, and were determined to have distinct catalytic activities. NF2152 releases a single product, β1,2-arabinobiose (Ara) from sugar beet arabinan (SBA), and β1,2-Ara and α-1,2-galactoarabinose (Gal-Ara) from rye arabinoxylan (RAX). NF2523 exclusively releases α-1,2-Gal-Ara from RAX, which represents the first description of a galacto-(α-1,2)-arabinosidase. Both β-1,2-Ara and α-1,2-Gal-Ara are disaccharides not previously described within SBA and RAX. In this regard, the enzymes studied here may represent valuable new biocatalytic tools for investigating the structures of rare arabinosyl-containing glycans, and potentially for facilitating their modification in industrial applications.

PubMed: 28588026
DOI: 10.1074/jbc.M117.789008

実験手法

X-RAY DIFFRACTION (1.748 Å)