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Structure-function studies can improve binding affinity of cohesin-dockerin interactions for multi-protein

Marlene Duarte1, Victor D Alves1, Márcia Correia2

  • 1CIISA-Centre for Interdisciplinary Research in Animal Health, Faculty of Veterinary Medicine, University of Lisbon, 1300-477 Lisbon, Portugal; Associate Laboratory for Animal and Veterinary Sciences (AL4AnimalS), 1300-477 Lisbon, Portugal.

International Journal of Biological Macromolecules
|October 17, 2022
PubMed
Summary

Researchers elucidated the dual-binding interaction of cohesin-dockerin modules in Ruminococcus flavefaciens cellulosomes. This discovery enables rational design for enhanced affinity in designer cellulosomes and biotechnology applications.

Keywords:
Biomass degradationCarbohydratesCellulosomeCohesinDockerinProtein complex

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Area of Science:

  • Biochemistry
  • Microbiology
  • Structural Biology

Background:

  • Cellulosomes are complex microbial enzyme systems crucial for degrading plant biomass.
  • Their intricate assembly relies on specific protein-protein interactions between cohesin (Coh) and dockerin (Doc) modules.
  • The Ruminococcus flavefaciens cellulosome exhibits exceptional complexity with unique Coh-Doc interaction modes.

Purpose of the Study:

  • To determine the structure of the ScaH Doc-ScaE Coh complex from R. flavefaciens.
  • To investigate the binding mode and identify key residues involved in Coh-Doc recognition.
  • To engineer Coh-Doc interactions for improved affinity and tailored applications.

Main Methods:

  • X-ray crystallography to determine the complex structure.
  • Site-directed mutagenesis to identify key residues.
  • Structure-informed protein engineering to modify binding affinity.

Main Results:

  • The ScaH Doc-ScaE Coh complex adopts a dual-binding mode, distinct from other type-III interactions in R. flavefaciens.
  • Key amino acid residues governing Coh recognition were identified.
  • Protein engineering successfully altered the electrostatic profile and enhanced Coh-Doc binding affinity.

Conclusions:

  • The binding interface of Coh-Doc modules significantly influences recognition and interaction specificity.
  • Coh-Doc affinity can be rationally modulated, offering potential for designing novel cellulosomes.
  • This work provides a foundation for developing advanced biomolecular technologies based on engineered protein interactions.