5FIP

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

Summary for 5FIP

• Entry DOI: 10.2210/pdb5fip/pdb
• Descriptor: GH5 CELLULASE, DI(HYDROXYETHYL)ETHER, TRIETHYLENE GLYCOL, ... (9 entities in total)
• Functional Keywords: hydrolase, cellulase, gh5
• Biological source: UNIDENTIFIED
• Total number of polymer chains: 4
• Total formula weight: 153434.59

Authors

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. (deposition date: 2015-10-01, release date: 2016-01-20, Last modification date: 2024-01-10)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.88 Å)