Evidence for a dual binding mode of dockerin modules to cohesins

@article{Carvalho2007EvidenceFA,
  title={Evidence for a dual binding mode of dockerin modules to cohesins},
  author={A. Carvalho and F. Dias and T. Nagy and J. Prates and M. Proctor and N. Smith and E. Bayer and G. Davies and L. Ferreira and M. Rom{\~a}o and C. Fontes and H. Gilbert},
  journal={Proceedings of the National Academy of Sciences},
  year={2007},
  volume={104},
  pages={3089 - 3094}
}
The assembly of proteins that display complementary activities into macromolecular complexes is critical to cellular function. One such enzyme complex, of environmental significance, is the plant cell wall degrading apparatus of anaerobic bacteria, termed the cellulosome. The complex assembles through the interaction of enzyme-derived “type I dockerin” modules with the multiple “cohesin” modules of the scaffolding protein. Clostridium thermocellum type I dockerin modules contain a duplicated 22… Expand
Functional asymmetry in cohesin binding belies inherent symmetry of the dockerin module: insight into cellulosome assembly revealed by systematic mutagenesis.
TLDR
The results suggest that the near-symmetry in sequence and structure of the repeated elements of the dockerin is not essential to cohesin binding, and that the observed plasticity in cohesIn-dockerin binding may facilitate cellulosome assembly in vivo or provide a conformational switch that promotes access of the tethered cellulosomal enzymes to their polysaccharide substrates. Expand
Novel Clostridium thermocellum Type I Cohesin-Dockerin Complexes Reveal a Single Binding Mode*
TLDR
The crystal structures of two novel Clostridium thermocellum type I cohesin-dockerin complexes revealed that the two dockerins, Doc918 and Doc124A, are unusual because they lack the structural symmetry required to support a dual binding mode. Expand
Combined Crystal Structure of a Type I Cohesin
TLDR
Combined computational modeling, mutagenesis, and affinity-based binding studies revealed similar hydrogen-bonding networks between putative Ser/Asp recognition residues in the dockerin at positions 11/12 and 45/46, suggesting that a dual-binding mode is not exclusive to the integration of enzymes into primary cellulosomes but can also characterize polycellulosome assembly and cell-surface attachment. Expand
Functional insights into the role of novel type I cohesin and dockerin domains from Clostridium thermocellum.
TLDR
The results revealed that Cthe_0452 is located at the C. thermocellum cell surface and thus the protein was renamed as OlpC, and the ligand specificities of the newly identified cohesin and dockerin domains are described. Expand
Dual binding in cohesin-dockerin complexes: the energy landscape and the role of short, terminal segments of the dockerin module
TLDR
The authors' molecular dynamics simulations of mechanical stretching of the full-length wild-type cohesin-dockerin complex indicate that each mode of binding leads to two kinds of stretching pathways, which may be mistakenly taken as evidence of dual binding. Expand
Analysis of cohesin-dockerin interactions using mutant dockerin proteins.
TLDR
Results suggest that the combination of the first and second dockerin segments is important for the target recognition of Clostridium josui cohesin modules. Expand
Atypical Cohesin-Dockerin Complex Responsible for Cell Surface Attachment of Cellulosomal Components
TLDR
A combined functional role for the three enigmatic dockerin inserts was established whereby these extraneous segments serve as structural buttresses that reinforce the stalklike conformation of the X-module, thus segregating its tethered complement of cellulosomal components from the cell surface. Expand
Escherichia coli expression, purification, crystallization, and structure determination of bacterial cohesin-dockerin complexes.
TLDR
Structural studies have revealed how the cohesin-dockerin interaction mediates cellulosome assembly and cell-surface attachment, while retaining the flexibility required to potentiate catalytic synergy within the complex. Expand
A dual cohesin–dockerin complex binding mode in Bacteroides cellulosolvens contributes to the size and complexity of its cellulosome
TLDR
The results indicate that, unlike other type II complexes, these possess a dual-binding mode of interaction, akin to type I complexes, which seems to play a pivotal role in the assembly of B. cellulosolvens cellulosome, which is consistent with its unmatched complexity and size. Expand
Cohesin‐dockerin microarray: Diverse specificities between two complementary families of interacting protein modules
TLDR
A microarray system for determining cohesin‐dockerin specificity is described, which allows global comparison among the interactions between various members of these two complementary families of interacting protein modules, and extensive cross‐species interaction among type‐II cohesins and dockerins is shown for the first time. Expand
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References

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Insights into the structural determinants of cohesin-dockerin specificity revealed by the crystal structure of the type II cohesin from Clostridium thermocellum SdbA.
TLDR
The crystal structure of the Type II cohesin (CohII) is reported from the Clostridium thermocellum cell surface anchoring protein SdbA, which is very similar to Type I cohesins, and the dockerin binding site is likely to be conserved in the two proteins. Expand
Cellulosome assembly revealed by the crystal structure of the cohesin–dockerin complex
  • A. Carvalho, F. Dias, +6 authors C. Fontes
  • Biology, Medicine
  • Proceedings of the National Academy of Sciences of the United States of America
  • 2003
TLDR
The structure provides an explanation for the lack of cross-species recognition between cohesin–dockerin pairs and thus provides a blueprint for the rational design, construction, and exploitation of these catalytic assemblies. Expand
The crystal structure of a type I cohesin domain at 1.7 A resolution.
TLDR
The crystal structure of a single cohesin domain from the scaffolding protein of Clostridium thermocellum is reported, which reveals no obvious Ca2+-binding site, and previous experiments have failed to detect high affinity binding ofCa2+ to the unliganded dockerin domain of endoglucanase CelD. Expand
Crystal structure of a cohesin module from Clostridium cellulolyticum: implications for dockerin recognition.
TLDR
A topology model of a C. cellulolyticum dockerin and a Cc-cohesin/dockerin complex is produced using homology modeling and available biochemical data and suggests that a special residue pair is located at the center of the cohesin surface putatively interacting with the dockerin. Expand
A cohesin domain from Clostridium thermocellum: the crystal structure provides new insights into cellulosome assembly.
TLDR
Three-dimensional crystal structure of one of the cohesin domains from C. thermocellum (cohesin 2) shows a nine-stranded beta sandwich with a jelly-roll topology, somewhat similar to the fold displayed by its neighboring cellulose-binding domain. Expand
Crystal structure of a type-II cohesin module from the Bacteroides cellulosolvens cellulosome reveals novel and distinctive secondary structural elements.
TLDR
The X-ray crystal structure of a type-II cohesin from scaffoldin A of Bacteroides cellulosolvens has been determined to a resolution of 1.6 angstroms using molecular replacement and suggests that each of the additional secondary structural elements assumes a flanking position relative to the putative dockerin-binding surface. Expand
Cohesin-Dockerin Interaction in Cellulosome Assembly
TLDR
The results indicate that mutation of a single residue from threonine to leucine at a given position of the C. thermocellum dockerin differentiates between its nonrecognition and high affinity recognition by a cohesin from Clostridium cellulolyticum, suggesting that the presence or absence of asingle decisive hydroxyl group is critical to the observed biorecognition. Expand
Duplicated dockerin subdomains of Clostridium thermocellum endoglucanase CelD bind to a cohesin domain of the scaffolding protein CipA with distinct thermodynamic parameters and a negative cooperativity.
TLDR
The binding affinity was strongly decreased when both segments were mutated, indicating strong negative cooperativity between the two mutated sites, and values show that cohesin-dockerin binding is mainly hydrophobic. Expand
A new type of cohesin domain that specifically binds the dockerin domain of the Clostridium thermocellum cellulosome-integrating protein CipA
TLDR
A new type of cohesin domain, which is present in one, two, and four copies in SdbA, ORF2p, and OlpB, respectively, can be defined. Expand
Probing the Mechanism of Ligand Recognition in Family 29 Carbohydrate-binding Modules*
TLDR
Mutagenesis reveals that “stacking” of tryptophan residues in the n and n+2 subsites plays a critical role in ligand binding, whereas the loss of tyrosine-mediated stacking in then+4 subsite reduces, but does not abrogate, polysaccharide recognition. Expand
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