Results 101 to 110 of about 139 (126)

Single versus dual-binding conformations in cellulosomal cohesin–dockerin complexes

Current Opinion in Structural Biology, 2016
Cohesins and dockerins are complementary interacting protein modules that form stable and highly specific receptor-ligand complexes. They play a crucial role in the assembly of cellulose-degrading multi-enzyme complexes called cellulosomes and have potential applicability in several technology areas, including biomass conversion processes.
Michael A Nash, Steven P Smith, Carlos MGA Fontes, Edward A Bayer   +3 more
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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
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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
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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
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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
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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
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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
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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
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Structure and function relationships in novel cohesin-dockerin complexes

2015
ABSTRACT - Relações estrutura-função em novos complexos coesina-doquerina. - As interacções coesina-doquerina são responsáveis pela organização de um complexo multi-enzimático concebido para a degradação de glúcidos complexos da parede celular vegetal e secretado por bactérias anaeróbias, denominado por celulossoma.
openaire   +1 more source

Constructing an Efficient Bacillus subtilis Spore Display by Using Cohesin−Dockerin Interactions

Molecules, 2021
Xiaomin Jiang
exaly