EC Number   |
Cofactor |
Reference |
|---|
   5.6.1.7 | GroES |
- |
750256, 750970, 751329, 752267 |
| 5.6.1.7 | GroES |
cofactor. ATP- and GroES-induced confinement within the GroEL cavity remodels bound polypeptides by causing expansion (or racking) of some regions and compaction of others, most notably, the hydrophobic core |
712763 |
| 5.6.1.7 | GroES |
GroE consists of the GroEL complex, an (alpha7)2 homoligomer with a dual-ring topology, and its homoheptameric cofactor, GroES, which acts as a lid for the GroEL folding chamber |
735006 |
| 5.6.1.7 | GroES |
GroEL and its bound cofactor GroES undergo an ATP-regulated interaction cycle that serves to close and open the folding cage. In the asymmetric reaction mode, only one ring of GroEL is GroES bound and the two rings function sequentially, coupled by negative allostery. In the symmetric mode, both GroEL rings are GroES bound and are folding active simultaneously. GroEL:GroES stoichiometry calculation: symmetric GroEL:GroES2 complexes are substantially populated only in the presence of non-foldable model proteins, such as alpha-lactalbumin and alpha-casein, which overstimulate the GroEL ATPase and uncouple the negative GroEL inter-ring allostery. In contrast, asymmetric complexes are dominant both in the absence of substrate and in the presence of foldable substrate proteins. Upon binding of ATP to GroEL, GroES caps the GroEL ring that holds the substrate (cis-ring), resulting in its displacement into an enclosed chamber large enough for proteins up to 60 kDa |
734487 |
| 5.6.1.7 | GroES |
GroES decreases the ATP hydrolysis rate of GroEL by 50% and exerts a greater inhibitory effect on GroELSR than GroEL, as it decreases ATP hydrolysis activity of GroELSR to 5-10% of the intrinsic rate of GroELSR. Interaction analysis between the single-ring GroELSR mutants and GroES, GroES cycles between association with and dissociation off the single-ring GroELSR variants. The diminished ATPase activity of the GroELSReGroES system is due to formation of a highly stable GroELSReGroES complex with a half life t1/2 of about 300 min |
733278 |
| 5.6.1.7 | GroES |
GroES forms a lid over the chamber, and in doing so dislodges bound substrate into the chamber, thereby allowing non-native proteins to fold in isolation. GroES also modulates allosteric transitions of the enzyme |
752285 |
| 5.6.1.7 | GroES |
the GroEL-GroES chaperonin machine is a nano-cage for protein folding, the apical GroEL domain (residues191-376) binds cofactor GroES. GroES is a dome-shaped heptameric ring of about 10 kDa subunits, binds to the ends of the GroEL cylinder, forming the cage in which the substrate protein is encapsulated for folding |
735322 |
| 5.6.1.7 | more |
GroES encapsulates substrate protein |
699525 |
