Results 121 to 130 of about 1,461 (191)

Evidence for a dual binding mode of dockerin modules to cohesins

open access: yes
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 ...
Carvalho AL   +11 more
core  

Cohesin-dockerin interaction based method to facilitate fast domain shuffling of cellobiohydrolases [PDF]

open access: yes, 2018
Mikrobien sellulaasit kuten sellobiohydrolaasit pystyvät hajottamaan selluloosaa ja lignoselluloosaista biomassaa pienemmiksi, glukoosia sisältäviksi monomeereiksi ja oligomeereiksi.
Kiviniemi, Eero A.
core  

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

open access: yesActa Crystallographica Section A Foundations of Crystallography, 2004
A. L. Carvalho   +7 more
openaire   +1 more source

Cellulosome assembly revealed by the crystal structure of the cohesin-dockerin complex

open access: yes
The utilization of organized supramolecular assemblies to exploit the synergistic interactions afforded by close proximity, both for enzymatic synthesis and for the degradation of recalcitrant substrates, is an emerging theme in cellular biology ...
Carvalho AL   +8 more
core  

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

open access: yes, 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.
Simpson P   +8 more
core  

Molecular architecture of modular (A) protein sequence with accession no. ABN54148.1 that comprises of N-terminal PL1A catalytic domain, followed by DOC, type-I dockerin and C terminal CBM6 binding domain.

open access: yes, 2015
(B) protein sequence with ac no. ABN53381.1 that comprises of N terminal PL1B catalytic domain, followed by DOC, type-I dockerin and CBM35 binding domain, with a C-terminal PL9 catalytic domain.
Maria S. J. Centeno (690514)   +7 more
core   +1 more source

Mapping by Site-Directed Mutagenesis of the Region Responsible for Cohesin−Dockerin Interaction on the Surface of the Seventh Cohesin Domain of Clostridium thermocellum CipA

open access: yes, 2002
International audienceTo locate the region involved in binding dockerin domains, 15 mutations were introduced across the surface of the seventh cohesin domain of the scaffolding protein CipA, which holds together the cellulosome of Clostridium ...
Miras, Isabelle   +3 more
core   +1 more source

Combined Crystal Structure of a Type I Cohesin: Mutation and Affinity Binding Studies Reveal Structural Determinants of Cohesin-Dockerin Specificities

open access: yes
Background: Cellulosomal cohesin-dockerin types are reversed in Bacteroides cellulosolvens. Results: Combined crystallographic and computational approaches of a lone cohesin yielded a structural model of the cohesin-dockerin complex that was verified ...
Cameron K   +10 more
core  

Insights into a type III cohesin-dockerin recognition interface from the cellulose-degrading bacterium Ruminococcus flavefaciens

open access: yes, 2015
Cellulosomes are large multicomponent cellulose-degrading assemblies found on the surfaces of cellulolytic microorganisms. Often containing hundreds of components, the self-assembly of cellulosomes is mediated by the ultra-high-affinity cohesin-dockerin ...
Lamed, Raphael   +14 more
core   +1 more source

Characterization of a Double Dockerin from the Cellulosome of the Anaerobic Fungus Piromyces equi

open access: yes
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 ...
Gilbert HJ   +5 more
core  

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