title: Single versus dual-binding conformations in cellulosomal cohesin-dockerin complexes.
abstract: 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.
authors: 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.
authors: Michael A
authors: MA
authors: Nash
authors: Department of Biomedical and Molecular Sciences, Queen's University, Kingston, Ontario K7L 3N6, Canada.
authors: Steven P
authors: SP
authors: Smith
authors: CIISA-Faculdade de Medicina Veterinária, ULisboa, Pólo Universitário do Alto da Ajuda, Avenida da Universidade Técnica, 1300-477 Lisboa, Portugal.
authors: Carlos Mga
authors: CM
authors: Fontes
authors: Department of Biological Chemistry, Weizmann Institute of Science, Rehovot 76100, Israel.
authors: Edward A
authors: EA
authors: Bayer
mesh_terms: D000818:Animals; D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism*; D018797:Cell Cycle Proteins / Q000737:chemistry* / Q000378:metabolism*; D044603:Cellulosomes / Q000378:metabolism*; D002868:Chromosomal Proteins, Non-Histone / Q000737:chemistry* / Q000378:metabolism*; D006801:Humans; D011485:Protein Binding; D011487:Protein Conformation; D013816:Thermodynamics; D000097722:Cohesins
chemical_list: D001426:Bacterial Proteins; D018797:Cell Cycle Proteins; D002868:Chromosomal Proteins, Non-Histone; D000097722:Cohesins