Results 161 to 170 of about 1,461 (191)

Phylogenomics and genetic analysis of solvent-producing Clostridium species. [PDF]

Sci Data
Jensen RO, Schulz F, Roux S, Klingeman DM, Mitchell WP, Udwary D, Moraïs S, Reynoso V, Winkler J, Nagaraju S, De Tissera S, Shapiro N, Ivanova N, Reddy TBK, Mizrahi I, Utturkar SM, Bayer EA, Woyke T, Mouncey NJ, Jewett MC, Simpson SD, Köpke M, Jones DT, Brown SD.   +23 more
europepmc   +1 more source

ez-CAZy a reference annotation database for linking glycoside hydrolase sequence to enzymatic activity. [PDF]

Sci Rep
Erdody DS, Griffin NG, Berlemont R.
europepmc   +1 more source

Evidence for a dual binding mode of dockerin modules to cohesins [PDF]

Proceedings of the National Academy of Sciences of the United States of America, 2007
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.
Ana Luisa Carvalho, Fernando M V Dias, JOSÉ A M Prates   +2 more
exaly   +4 more sources

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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
openaire   +3 more sources

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
Chao Chen, Jinsong Xuan, Qiu Cui
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 ...
Silvia Spinelli, Henri-Pierre Fierobe, Bernard Henrissat   +2 more
exaly   +3 more sources

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
openaire   +1 more source

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
openaire   +2 more sources