5FIP

Discovery and characterization of a novel thermostable and highly halotolerant GH5 cellulase from an Icelandic hot spring isolate

5FIP の概要

• エントリーDOI: 10.2210/pdb5fip/pdb
• 分子名称: GH5 CELLULASE, DI(HYDROXYETHYL)ETHER, TRIETHYLENE GLYCOL, ... (9 entities in total)
• 機能のキーワード: hydrolase, cellulase, gh5
• 由来する生物種: UNIDENTIFIED
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 153434.59

構造登録者

Zarafeta, D.,Kissas, D.,Sayer, C.,Gudbergsdottir, S.R.,Ladoukakis, E.,Isupov, M.N.,Chatziioannou, A.,Peng, X.,Littlechild, J.A.,Skretas, G.,Kolisis, F.N. (登録日: 2015-10-01, 公開日: 2016-01-20, 最終更新日: 2024-01-10)

主引用文献

Zarafeta, D.,Kissas, D.,Sayer, C.,Gudbergsdottir, S.R.,Ladoukakis, E.,Isupov, M.N.,Chatziioannou, A.,Peng, X.,Littlechild, J.A.,Skretas, G.,Kolisis, F.N.
Discovery and Characterization of a Thermostable and Highly Halotolerant Gh5 Cellulase from an Icelandic Hot Spring Isolate.
Plos One, 11:46454-, 2016

PubMed Abstract: With the ultimate goal of identifying robust cellulases for industrial biocatalytic conversions, we have isolated and characterized a new thermostable and very halotolerant GH5 cellulase. This new enzyme, termed CelDZ1, was identified by bioinformatic analysis from the genome of a polysaccharide-enrichment culture isolate, initiated from material collected from an Icelandic hot spring. Biochemical characterization of CelDZ1 revealed that it is a glycoside hydrolase with optimal activity at 70°C and pH 5.0 that exhibits good thermostability, high halotolerance at near-saturating salt concentrations, and resistance towards metal ions and other denaturing agents. X-ray crystallography of the new enzyme showed that CelDZ1 is the first reported cellulase structure that lacks the defined sugar-binding 2 subsite and revealed structural features which provide potential explanations of its biochemical characteristics.

PubMed: 26741138
DOI: 10.1371/JOURNAL.PONE.0146454

実験手法

X-RAY DIFFRACTION (1.88 Å)