DOI: 10.1073/pnas.0611173104. Evidence for a dual binding mode of dockerin modules to cohesins

Evidence for a dual binding mode of dockerin modules to cohesins

10.1073/pnas.0611173104

Crossref journal-article

Proceedings of the National Academy of Sciences

Proceedings of the National Academy of Sciences (341)

Abstract

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-residue sequence that comprises helix-1 and helix-3, respectively. The crystal structure of a C. thermocellum type I cohesin-dockerin complex showed that cohesin recognition was predominantly through helix-3 of the dockerin. The sequence duplication is reflected in near-perfect 2-fold structural symmetry, suggesting that both repeats could interact with cohesins by a common mechanism in wild-type (WT) proteins. Here, a helix-3 disrupted mutant dockerin is used to visualize the reverse binding in which the dockerin mutant is indeed rotated 180° relative to the WT dockerin such that helix-1 now dominates recognition of its protein partner. The dual binding mode is predicted to impart significant plasticity into the orientation of the catalytic subunits within this supramolecular assembly, which reflects the challenges presented by the degradation of a heterogeneous, recalcitrant, insoluble substrate by a tethered macromolecular complex.

Bibliography

Carvalho, A. L., Dias, F. M. V., Nagy, T., Prates, J. A. M., Proctor, M. R., Smith, N., Bayer, E. A., Davies, G. J., Ferreira, L. M. A., RomÃ£o, M. J., Fontes, C. M. G. A., & Gilbert, H. J. (2007). Evidence for a dual binding mode of dockerin modules to cohesins. Proceedings of the National Academy of Sciences, 104(9), 3089â3094.

Authors 12

Ana Luísa Carvalho (first)
Fernando M. V. Dias (additional)
Tibor Nagy (additional)
José A. M. Prates (additional)
Mark R. Proctor (additional)
Nicola Smith (additional)
Edward A. Bayer (additional)
Gideon J. Davies (additional)
Luís M. A. Ferreira (additional)
Maria J. Romão (additional)
Carlos M. G. A. Fontes (additional)
Harry J. Gilbert (additional)

References 42 Referenced 131

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Dates

Type	When
Created	18 years, 6 months ago (Feb. 21, 2007, 12:04 a.m.)
Deposited	3 years, 4 months ago (April 12, 2022, 3:57 p.m.)
Indexed	1 week ago (Aug. 29, 2025, 6:11 a.m.)
Issued	18 years, 6 months ago (Feb. 27, 2007)
Published	18 years, 6 months ago (Feb. 27, 2007)
Published Online	18 years, 6 months ago (Feb. 27, 2007)
Published Print	18 years, 6 months ago (Feb. 27, 2007)

Funders 0

None

BibTeX

@article{Carvalho_2007, title={Evidence for a dual binding mode of dockerin modules to cohesins}, volume={104}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.0611173104}, DOI={10.1073/pnas.0611173104}, number={9}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Carvalho, Ana Luísa and Dias, Fernando M. V. and Nagy, Tibor and Prates, José A. M. and Proctor, Mark R. and Smith, Nicola and Bayer, Edward A. and Davies, Gideon J. and Ferreira, Luís M. A. and Romão, Maria J. and Fontes, Carlos M. G. A. and Gilbert, Harry J.}, year={2007}, month=feb, pages={3089–3094} }

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