Cohesin–dockerin interaction in cellulosome assembly: a single Asp‐to‐Asn mutation disrupts high‐affinity cohesin–dockerin binding
Copyright policy )Cohesin–dockerin interaction in cellulosome assembly: a single Asp‐to‐Asn mutation disrupts high‐affinity cohesin–dockerin binding
The cohesive cellulosome complex is sustained by the high‐affinity cohesin–dockerin interaction. In previous work [J. Biol. Chem. 276 (2001) 9883], we demonstrated that a single Thr‐to‐Leu replacement in the Clostridium thermocellum dockerin component differentiates between non‐recognition and high‐affinity recognition by the interspecies rival cohesin from C. cellulolyticum. In this report, we show that a single Asp‐to‐Asn substitution on the cohesin counterpart also disrupts normal recognition of the dockerin. The Asp34 carboxyl group of the cohesin appears to play a central role in the resultant hydrogen‐bonding network as an acceptor of two crucial hydrogen bonds from Ser45 of the dockerin domain. The results underscore the fragile nature of the intermolecular contact interactions that maintain this very high‐affinity protein–protein interaction.
Models, Molecular, Chromosomal Proteins, Non-Histone, Protein Conformation, Molecular Sequence Data, Mutation, Missense, Cell Cycle Proteins, Enzyme-Linked Immunosorbent Assay, Cohesin–dockerin binding specificity, Clostridium thermocellum, Fungal Proteins, Bacterial Proteins, Amino Acid Sequence, Cohesins, Clostridium, Sequence Homology, Amino Acid, Nuclear Proteins, Protein–protein interaction, Kinetics, Amino Acid Substitution, Clostridium cellulolyticum, Carrier Proteins, Sequence Alignment, Cellulosome, Multi-enzyme complex, Protein Binding
Models, Molecular, Chromosomal Proteins, Non-Histone, Protein Conformation, Molecular Sequence Data, Mutation, Missense, Cell Cycle Proteins, Enzyme-Linked Immunosorbent Assay, Cohesin–dockerin binding specificity, Clostridium thermocellum, Fungal Proteins, Bacterial Proteins, Amino Acid Sequence, Cohesins, Clostridium, Sequence Homology, Amino Acid, Nuclear Proteins, Protein–protein interaction, Kinetics, Amino Acid Substitution, Clostridium cellulolyticum, Carrier Proteins, Sequence Alignment, Cellulosome, Multi-enzyme complex, Protein Binding
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