PDBsum entry 5fip

Hydrolase

PDB id: 5fip

Contents

Protein chains

331 a.a.

Ligands

PEG ×11

PGE ×4

EDO ×18

IPA ×13

PG6

PG4

Metals

_CL ×7

Waters ×585

References listed in PDB file

Key reference

• Title: Discovery and characterization of a thermostable and highly halotolerant gh5 cellulase from an icelandic hot spring isolate.
• Authors: D.Zarafeta, D.Kissas, C.Sayer, S.R.Gudbergsdottir, E.Ladoukakis, M.N.Isupov, A.Chatziioannou, X.Peng, J.A.Littlechild, G.Skretas, F.N.Kolisis.
• Ref.: Plos One, 2016, 11, e0146454. [DOI no: 10.1371/journal.pone.0146454]
• PubMed id: 26741138

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.