CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.60 | 4-Layer Sandwich |
|
3.60.20 | Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 |
|
3.60.20.10 | Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 |
Domain Context
CATH Clusters
| Superfamily | Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 |
| Functional Family | ATP-dependent protease subunit HslV |
Enzyme Information
| 3.4.25.2 |
HslU--HslV peptidase.
based on mapping to UniProt P0A7B8
ATP-dependent cleavage of peptide bonds with broad specificity.
-!- The HslU subunit of the HslU--HslV complex functions as an ATP dependent 'unfoldase'. -!- The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. -!- HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. -!- Belongs to peptidase family T1.
|
UniProtKB Entries (1)
| P0A7B8 |
HSLV_ECOLI
Escherichia coli K-12
ATP-dependent protease subunit HslV
|
PDB Structure
| PDB | 4G4E |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Structural Alteration in the Pore Motif of the Bacterial 20S Proteasome Homolog HslV Leads to Uncontrolled Protein Degradation
J.Mol.Biol.
|