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Cellulosome assembly and the crystal structure of the cohesin–dockerin complex [PDF]

Acta Crystallographica Section A Foundations of Crystallography, 2004
A. L. Carvalho, F. M. V. Dias, J. A. M. Prates, T. Nagy, H. J. Gilbert, G. J. Davies, C. M. G. A. Fontes, M. J. Romao   +7 more
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Unconventional Cohesin-Dockerin binding mechanisms reveal the complexity of cellulosome assembly

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Scaffoldin-Modified Silk for Specific Immobilization of Dockerin-Fused Enzymes

Journal of Insect Biotechnology and Sericology
Sumitani, Megumi, Watanabe, Hirofumi, Iga, Masatoshi, Iizuka, Tetsuya   +3 more
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Resonance assignments of a cellulosomal double-dockerin from Clostridium thermocellum

Biomolecular NMR Assignments, 2018
Cellulosomes are highly efficient multienzyme complexes for lignocellulose degradation secreted by some lignocellulolytic bacteria. Cellulosomes are assembled through protein modules named cohesin and dockerin, and multiple cohesin modules in the scaffold protein generally determine the complexity of the cellulosomes. Some cellulosomal proteins contain
Yingang Feng, Jinsong Xuan, Chao Chen
exaly   +3 more sources

Crystal structure of a cohesin module from Clostridium cellulolyticum: implications for dockerin recognition

Journal of Molecular Biology, 2000
In the assembly of the Clostridium cellulolyticum cellulosome, the multiple cohesin modules of the scaffolding protein CipC serve as receptors for cellulolytic enzymes which bear a dockerin module. The X-ray structure of a type I C. cellulolyticum cohesin module (Cc-cohesin) has been solved using molecular replacement, and refined at 2.0 A resolution ...
Christian Cambillau, Bernard Henrissat, Silvia Spinelli   +2 more
exaly   +3 more sources

Species-specificity of the cohesin-dockerin interaction betweenClostridium thermocellum andClostridium cellulolyticum: Prediction of specificity determinants of the dockerin domain

Proteins: Structure, Function, and Genetics, 1997
The cross-species specificity of the cohesin-dockerin interaction, which defines the incorporation of the enzymatic subunits into the cellulosome complex, has been investigated. Cohesin-containing segments from the cellulosomes of two different species, Clostridium thermocellum and Clostridium cellulolyticum, were allowed to interact with cellulosomal (
S, Pagès, A, Bélaïch, J P, Bélaïch, E, Morag, R, Lamed, Y, Shoham, E A, Bayer   +6 more
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Cohesin-Dockerin Interactions and Folding

2014
Many investigations were conducted to characterize the cohesin-dockerin interactions. These studies include measuring cohesin-dockerin affinity, identifying critical amino acid residues by site-directed mutagenesis, and determining the molecular structures of the dockerin, cohesin, and its complex.
J. H. David Wu, Michael Newcomb, Kazuo Sakka   +2 more
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Cohesin-dockerin recognition in cellulosome assembly: Experiment versus hypothesis

Proteins: Structure, Function, and Genetics, 2000
The cohesin-dockerin interaction provides the basis for incorporation of the individual enzymatic subunits into the cellulosome complex. In a previous article (Pagés et al., Proteins 1997;29:517-527) we predicted that four amino acid residues of the approximately 70-residue dockerin domain would serve as recognition codes for binding to the cohesin ...
A, Mechaly, S, Yaron, R, Lamed, H P, Fierobe, A, Belaich, J P, Belaich, Y, Shoham, E A, Bayer   +7 more
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Characterization of a Double Dockerin from the Cellulosome of the Anaerobic Fungus Piromyces equi

Journal of Molecular Biology, 2007
The assembly into supramolecular complexes of proteins having complementary activities is central to cellular function. One such complex of considerable biological and industrial significance is the plant cell wall-degrading apparatus of anaerobic microorganisms, termed the cellulosome.
Nagy T, Tunnicliffe RB, Higgins LD, Walters C, Gilbert HJ, Williamson MP   +5 more
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Resonance assignments of cohesin and dockerin domains from Clostridium acetobutylicum ATCC824

Biomolecular NMR Assignments, 2012
Cohesin and dockerin domains are critical assembling components of cellulosome, a large extracellular multienzyme complex which is used by anaerobic cellulolytic bacteria to efficiently degrade lignocellulose. According to sequence homology, cohesins can be divided into three major groups, whereas cohesins from Clostridium acetobutylicum are beyond ...
Zhenling, Cui, Yifei, Li, Yan, Xiao, Yingang, Feng, Qiu, Cui, Qui, Cui   +5 more
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