 |
PDBsum entry 5fip
|
|
|
|
PDB id:
|
|
|
|
| Name: |
|
Hydrolase
|
|
|
Title:
|
|
Discovery and characterization of a novel thermostable and highly halotolerant gh5 cellulase from an icelandic hot spring isolate
|
|
Structure:
|
|
Gh5 cellulase. Chain: a, b, c, d. Ec: 3.2.1.4
|
|
Source:
|
|
Unidentified. Organism_taxid: 32644. Other_details: icelandic hot spring isolate
|
|
Resolution:
|
|
|
1.88Å
|
R-factor:
|
0.195
|
R-free:
|
0.234
|
|
|
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
|
|
Key ref:
|
|
D.Zarafeta
et al.
(2016).
Discovery and Characterization of a Thermostable and Highly Halotolerant GH5 Cellulase from an Icelandic Hot Spring Isolate.
Plos One,
11,
e0146454.
PubMed id:
DOI:
|
|
|
Date:
|
|
|
01-Oct-15
|
Release date:
|
20-Jan-16
|
|
|
|
|
|
|
PROCHECK
|
|
|
|
|
|
Headers
|
|
|
|
References
|
|
|
|
|
|
|
|
I3VS73
(I3VS73_THESW) -
cellulase from Thermoanaerobacterium saccharolyticum (strain DSM 8691 / JW/SL-YS485)
|
|
|
|
Seq:
Struc:
|
|
|
|
385 a.a.
331 a.a.*
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Key: |
 |
PfamA domain |
|
|
 |
Secondary structure |
|
 |
CATH domain |
|
|
*
PDB and UniProt seqs differ
at 10 residue positions (black
crosses)
|
|
|
|
|
|
|
|
|
|
|
|
|
Enzyme class:
|
|
E.C.3.2.1.4
- cellulase.
|
|
|
|
|
|
|
Reaction:
|
|
Endohydrolysis of 1,4-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
| |
|
DOI no:
|
Plos One
11:e0146454
(2016)
|
|
PubMed id:
|
|
|
|
|
|
| |
|
Discovery and Characterization of a Thermostable and Highly Halotolerant GH5 Cellulase from an Icelandic Hot Spring Isolate.
|
|
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.
|
|
|
|
|
| |
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.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
 |
 |
|
Links
