Results 171 to 180 of about 1,461 (191)

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
openaire   +4 more sources

Dual binding mode in cohesin-dockerin complexes as assessed through stretching studies

The Journal of Chemical Physics, 2016
A recent experimental study by Jobst et al. of stretching of a wild-type (WT) cohesin-dockerin complex has identified two kinds of the force-displacement patterns, with a single or double-peaked final rupture, which are termed “short” and “long” here. This duality has been interpreted as arising from the existence of two kinds of binding.
Michał Wojciechowski, Marek Cieplak
openaire   +2 more sources

Cellulosome from Clostridium cellulolyticum: Molecular Study of the Dockerin/Cohesin Interaction

Biochemistry, 1999
Clostridium cellulolyticum produces cellulolytic complexes (cellulosomes) made of 10-13 cell wall degrading enzymes tightly bound to a scaffolding protein (CipC) by means of their dockerin domain. It has previously been shown that the receptor domains in CipC are the cohesin domains and that the cohesin/dockerin interaction is calcium-dependent. In the
H P, Fierobe, S, Pagès, A, Bélaïch, S, Champ, D, Lexa, J P, Bélaïch   +5 more
openaire   +2 more sources

Correlated mutations: Advances and limitations. A study on fusion proteins and on the Cohesin‐Dockerin families

Proteins: Structure, Function, and Bioinformatics, 2006
AbstractCorrelated mutations have been repeatedly exploited for intramolecular contact map prediction. Over the last decade these efforts yielded several methods for measuring correlated mutations. Nevertheless, the application of correlated mutations for the prediction of intermolecular interactions has not yet been explored.
Inbal, Halperin, Haim, Wolfson, Ruth, Nussinov   +2 more
openaire   +2 more sources

Flexibility and specificity of the cohesin–dockerin interaction: implications for cellulosome assembly and functionality

Biocatalysis and Biotransformation, 2012
Cellulosomes are highly elaborate multi-enzyme complexes of Carbohydrate Active enZYmes (CAZYmes) secreted by cellulolytic microorganisms, which very effectively degrade the most abundant polymers on Earth, cellulose and hemicelluloses. Cellulosome assembly requires that a non-catalytic dockerin module found in cellulosomal enzymes binds to one of the ...
Benedita Andrade Pinheiro, Joana Luís Armada Brás, Shabir Najmudin, Ana Luísa Carvalho, Luís M. A. Ferreira, José A. M. Prates, Carlos Mendes Godinho Andrade Fontes   +6 more
openaire   +1 more source

Characterization of a dockerin‐based affinity tag: application for purification of a broad variety of target proteins

Journal of Molecular Recognition, 2010
AbstractCellulose, a major component of plant matter, is degraded by a cell surface multiprotein complex called the cellulosome produced by several anaerobic bacteria. This complex coordinates the assembly of different glycoside hydrolases, via a high‐affinity Ca2+‐dependent interaction between the enzyme‐borne dockerin and the scaffoldin‐borne cohesin
Alik, Demishtein, Alon, Karpol, Yoav, Barak, Raphael, Lamed, Edward A, Bayer   +4 more
openaire   +2 more sources

Escherichia coli Expression, Purification, Crystallization, and Structure Determination of Bacterial Cohesin–Dockerin Complexes

2012
Cellulosomes are highly efficient nanomachines that play a fundamental role during the anaerobic deconstruction of complex plant cell wall carbohydrates. The assembly of these complex nanomachines results from the very tight binding of repetitive cohesin modules, located in a noncatalytic molecular scaffold, and dockerin domains located at the C ...
Bras JLA, Carvalho AL, Viegas A, Najmudin S, Alves VD, Prates JAM, Ferreira LMA, Romao MJ, Gilbert HJ, Fontes CMGA   +9 more
openaire   +3 more sources

Characterization of a cellulosome dockerin domain from the anaerobic fungus Piromyces equi.

Nature structural biology, 2001
The recycling of photosynthetically fixed carbon in plant cell walls is a key microbial process. In anaerobes, the degradation is carried out by a high molecular weight multifunctional complex termed the cellulosome. This consists of a number of independent enzyme components, each of which contains a conserved dockerin domain, which functions to bind ...
Raghothama S, Eberhardt RY, Simpson P, Wigelsworth D, White P, Hazlewood GP, Nagy T, Gilbert HJ, Williamson MP   +8 more
openaire   +2 more sources

Cohesin-dockerin code in cellulosomal dual binding modes and its allosteric regulation by proline isomerization

Structure, 2021
Andres Manuel Vera, Albert Galera-Prat, Michał Wojciechowski   +2 more
exaly  

Analysis of cohesin-dockerin interactions using mutant dockerin proteins

FEMS Microbiology Letters, 2011
Kazuo Sakka, Sadanari Jindou, Makiko Sakka   +2 more
exaly