Results 51 to 60 of about 5,379 (199)
Heterotropic regulation and negative homotropic cooperativity
FEBS Open Bio, EarlyView.We identified a structural module common to some proteins that couple negative cooperativity with heterotropic regulation, two features that rarely coexist. These proteins are ring‐like and present an ordered asymmetry whereby noncontacting subunits are symmetric, and their tertiary structure differs from that of contacting subunits.
Veronica Morea +5 more
wiley +1 more source
Chloroplast Chaperonin: An Intricate Protein Folding Machine for Photosynthesis
Frontiers in Molecular Biosciences, 2018 Group I chaperonins are large cylindrical-shaped nano-machines that function as a central hub in the protein quality control system in the bacterial cytosol, mitochondria and chloroplasts.
Qian Zhao, Qian Zhao, Cuimin Liu
doaj +1 more source
A minimal cellulosome‐like system in Cellulosilyticum lentocellum
FEBS Open Bio, EarlyView.Cellulose‐degrading bacteria typically use cellulosomes, large multi‐enzyme complexes on a scaffold protein. In Cellulosilyticum lentocellum, we characterise a far smaller arrangement, a single scaffold bound to one cellulase through a single cohesin‐dockerin interaction.
John Allan +2 more
wiley +1 more source
Mechanism of Action of Group II Chaperonins: [PDF]
, 2007 Chaperonins are highly allosteric double-ring ATPases that mediate cellular protein folding. ATP binding and hydrolysis control opening and closing of the central chaperonin chamber which transiently provides a protected environment for protein folding ...
Reißmann, Stefanie
core +1 more source
FEBS Open Bio, EarlyView.Functional screening identified PcSyn14890, a cyanobacteria‐specific protein that enhances growth and stress resistance in E. coli and Synechocystis PCC6803. Although we expected it to function as a molecular chaperone, it was unable to protect against thermal aggregation of GAPDH.
Akiyo Yamada +7 more
wiley +1 more source
Opening Up the Group II Chaperonins [PDF]
, 2010 A new study in this issue of Structure (Huo et al., 2010) reports the crystal structure of a group II chaperonin in the open state, providing unprecedented levels of detail for the domain movements that result from ATP hydrolysis and a clearer picture of
Rao, Zihe, Zihe Rao
core +1 more source
Single-molecule fluorescence polarization study of conformational change in archaeal group II chaperonin. [PDF]
PLoS ONE, 2011 Group II chaperonins found in archaea and in eukaryotic cytosol mediate protein folding without a GroES-like cofactor. The function of the cofactor is substituted by the helical protrusion at the tip of the apical domain, which forms a built-in lid on ...
Ryo Iizuka +3 more
doaj +1 more source
American Journal of Medical Genetics Part A, EarlyView.ABSTRACT Genetic modifiers of Duchenne muscular dystrophy (DMD) that alter disease severity or response to therapy have been reported using natural history or registry data sets of older corticosteroid‐treated patients. We tested associations of genetic modifiers on motor function outcomes in young (4 to < 7 years) steroid naïve clinical trial ...
Utkarsh J. Dang +16 more
wiley +1 more source
The thermosome: archetype of group II chaperonins [PDF]
, 1998 The thermosome, the chaperonin of the archaea, and its homologue from the cytosol of eukaryotes, known as TRiC or CCT, form a distinct subfamily of the chaperonins that does not depend on a co-chaperonin for protein folding activity.
Baumeister, Wolfgang +5 more
core +1 more source
Nature Communications, 2017 Chaperonins (CPNs) are ATP-dependent protein-folding machines. Here the authors present the open and closed crystal structures of a Group III CPN from the thermophilic bacterium Carboxydothermus hydrogenoformans, discuss its mechanism and structurally ...
Young Jun An +8 more
doaj +1 more source