Combined SAXS and computational approaches for structure determination and binding characteristics of Chimera (CtGH1-L1-CtGH5-F194A) generated by assembling β-glucosidase (CtGH1) and a mutant endoglucanase (CtGH5-F194A) from Clostridium thermocellum.
Amino Acid Sequence
beta-Glucosidase
/ metabolism
Binding Sites
/ physiology
Catalytic Domain
/ physiology
Cellulase
/ metabolism
Clostridium thermocellum
/ metabolism
Hydrolysis
Molecular Dynamics Simulation
Oligosaccharides
/ metabolism
Protein Binding
/ physiology
Protein Structure, Secondary
Scattering, Small Angle
Thermodynamics
X-Ray Diffraction
/ methods
Chimera
MD simulation
SAXS
Journal
International journal of biological macromolecules
ISSN: 1879-0003
Titre abrégé: Int J Biol Macromol
Pays: Netherlands
ID NLM: 7909578
Informations de publication
Date de publication:
01 Apr 2020
01 Apr 2020
Historique:
received:
01
10
2019
revised:
10
01
2020
accepted:
11
01
2020
pubmed:
17
1
2020
medline:
15
12
2020
entrez:
17
1
2020
Statut:
ppublish
Résumé
Chimera (CtGH1-L1-CtGH5-F194A) developed by fusing β-glucosidase (CtGH1) at N-terminal and endoglucanase (CtGH5-F194A) at C-terminal was structurally characterized. Its secondary structure analysis by CD showed 38% α-helix, 9.3% β-sheets and 52.7% random coils corroborating with prediction. In-silico modeled structure of Chimera comprised two modules, CtGH1 and CtGH5-F194A displaying (α/β)
Identifiants
pubmed: 31945441
pii: S0141-8130(19)37938-3
doi: 10.1016/j.ijbiomac.2020.01.116
pii:
doi:
Substances chimiques
beta-Glucosidase
EC 3.2.1.21
cellohexaose
2478-35-5
Cellulase
EC 3.2.1.4
Oligosaccharides
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
364-377Informations de copyright
Copyright © 2020 Elsevier B.V. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of competing interest The authors declare that they have no conflicts of interest with the content of this article.