Any feedback?
Literature summary for 5.6.1.7 extracted from
- Crystal structure of the native chaperonin complex from Thermus thermophilus revealed unexpected asymmetry at the cis-cavity (2004), Structure, 12, 1471-1480.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| crystal structure of the native GroEL-GroES-ADP homolog with substrate proteins in the cis-cavity, at 2.8 A resolution. Twenty-four in vivo substrate proteins within the cis-cavity are identified from the crystals | Thermus thermophilus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Thermus thermophilus | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | the chaperonins GroEL and GroES are essential mediators of protein folding. GroEL binds nonnative protein, ATP, and GroES, generating a ternary complex in which protein folding occurs within the cavity capped by GroES | Thermus thermophilus | ? | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| GroEL-GroES-ADP homolog | - |
Thermus thermophilus |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
