Any feedback?
Literature summary for 3.4.25.2 extracted from
- A structurally dynamic region of the HslU intermediate domain controls protein degradation and ATP hydrolysis (2016), Structure, 24, 1766-1777 .
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| L199Q | substitution in I-domain of subunit HslU. Mutation does not alter the structure of the AAA+ ring or its interactions with HslV but increases I-domain susceptibility to limited endoproteolysis. The mutation increases the rate of ATP-hydrolysis substantially, results in slower degradation of some proteins but faster degradation of other substrates, and markedly changes the preference of HslUV for initiating degradation at the N-terminus or C-terminus of model substrates | Escherichia coli |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | P0A6H5 and P0A7B8 | P0A6H5 i.e. subunit HslU, P0A7B8 i.e. subunit HslV | - |
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
