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Single versus dual-binding conformations in cellulosomal cohesin-dockerin complexes.
Journal article

Single versus dual-binding conformations in cellulosomal cohesin-dockerin complexes.

  • Nash MA Lehrstuhl für Angewandte Physik and Center for Nanoscience, Ludwig-Maximilians-Universität, 80799 Munich, Germany; Department of Chemistry, University of Basel, 4056 Basel, Switzerland; Department of Biosystems Science and Engineering, Eidgenössische Technische Hochschule (ETH-Zürich), 4058 Basel, Switzerland. Electronic address: michael.nash@unibas.ch.
  • Smith SP Department of Biomedical and Molecular Sciences, Queen's University, Kingston, Ontario K7L 3N6, Canada.
  • Fontes CM CIISA-Faculdade de Medicina Veterinária, ULisboa, Pólo Universitário do Alto da Ajuda, Avenida da Universidade Técnica, 1300-477 Lisboa, Portugal.
  • Bayer EA Department of Biological Chemistry, Weizmann Institute of Science, Rehovot 76100, Israel.
  • 2016-09-01
Published in:
  • Current opinion in structural biology. - 2016
Animals
Bacterial Proteins
Cell Cycle Proteins
Cellulosomes
Chromosomal Proteins, Non-Histone
Humans
Protein Binding
Protein Conformation
Thermodynamics
English Cohesins and dockerins are complementary interacting protein modules that form stable and highly specific receptor-ligand complexes. They play a crucial role in the assembly of cellulose-degrading multi-enzyme complexes called cellulosomes and have potential applicability in several technology areas, including biomass conversion processes. Here, we describe several exceptional properties of cohesin-dockerin complexes, including their tenacious biochemical affinity, remarkably high mechanostability and a dual-binding mode of recognition that is contrary to the conventional lock-and-key model of receptor-ligand interactions. We focus on structural aspects of the dual mode of cohesin-dockerin binding, highlighting recent single-molecule analysis techniques for its explicit characterization.
Language
  • English
Open access status
closed
Identifiers
Persistent URL
https://sonar.ch/global/documents/68223
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