Structural and functional characterization of a novel type-III dockerin fromRuminococcus flavefaciens

Autor: Ilit Noach, Maroor K. Jobby, Alon Karpol, Steven P. Smith, Edward A. Bayer, Michal Slutzki, Seth Chitayat
Rok vydání: 2012
Předmět:
Protein Folding
Circular dichroism
Chromosomal Proteins
Non-Histone
Surface Properties
Biophysics
Cell Cycle Proteins
Dockerin
Cellulosomes
Biology
Biochemistry
Protein–protein interaction
Cellulosome
03 medical and health sciences
Bacterial Proteins
Structural Biology
Ruminococcus
Genetics
Protein Interaction Domains and Motifs
Ruminococcus flavefaciens
EF Hand Motifs
Nuclear Magnetic Resonance
Biomolecular
Molecular Biology
Phylogeny
030304 developmental biology
Cohesin
0303 health sciences
Binding Sites
Calorimetry
Differential Scanning
030306 microbiology
Circular Dichroism
Calcium-Binding Proteins
Scaffoldin
Isothermal titration calorimetry
Cell Biology
Nuclear magnetic resonance spectroscopy
Recombinant Proteins
Spectrometry
Fluorescence
Multiprotein Complexes
Calcium
biological phenomena
cell phenomena
and immunity
Hydrophobic and Hydrophilic Interactions
Zdroj: FEBS Letters. 587:30-36
ISSN: 0014-5793
DOI: 10.1016/j.febslet.2012.11.012
Popis: Phylogenetic analysis of known dockerins in Ruminococcus flavefaciens revealed a novel subtype, type-Ill, in the scaffoldin proteins, ScaA, ScaB, ScaC and ScaE. In this study, we explored the Ca 2+ -binding properties of the type-Ill dockerin from the ScaA scaffoldin (ScaADoc) using a battery of structural and biophysical approaches including circular dichroism spectroscopy, isothermal titration calorimetry, differential scanning calorimetry, and nuclear magnetic resonance spectroscopy. Despite the lack of a second canonical Ca 2+ -binding loop, the behaviour of ScaADoc is similar with respect to other dockerin protein modules in terms of its responsiveness to Ca 2+ and affinity for the cohesin from the ScaB scaffoldin. Our results highlight the robustness of dockerin modules and how their Ca 2+ -binding properties can be exploited in the construction of designer cellulosomes. Structured summary of protein interactions ScaB cohesin and ScaADoc bind by isothermal titration calorimetry ( View interaction ) ScaB cohesin and ScaADoc bind by molecular sieving ( View interaction ) ScaADoc and ScaB cohesin bind by biophysical ( View interaction ) ScaB cohesin binds to ScaADoc by enzyme linked immunosorbent assay ( View interaction )
Databáze: OpenAIRE
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