› 6pxk

X-ray diffraction
3.65Å resolution

3.65 Angstroms resolution structure of HslU with an axial-channel plug

Released:
DOI: 10.2210/pdb6pxk/pdb
PDB entry 6pxk coloured by chain, front view.
PDB entry 6pxk coloured by chain, side view.
PDB entry 6pxk coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Heat activates the AAA+ HslUV protease by melting an axial autoinhibitory plug.
Baytshtok V, Fei X, Shih TT, Grant RA, Santos JC, Baker TA, Sauer RT
OpenAccess logo Cell Rep 34 108639 (2021)
PMID: 33472065

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assemblies composition:
hetero heptamer (preferred)
homo hexamer
Assembly name:
PDBe Complex ID:
PDB-CPX-531857 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
ATP-dependent protease ATPase subunit HslU Chains: A, B, C, D, E, F, G, H, I, J, K, L
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L
Length: 448 amino acids
Theoretical weight: 50.97 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A6H5 (Residues: 2-443; Coverage: 100%)
Gene names: JW3902, b3931, hslU, htpI
Sequence domains:
unidentified alpha helical sequence Chain: X
Molecule details ›
Chain: X
Length: 16 amino acids
Theoretical weight: 1.38 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli

Ligands and Environments

2 bound ligands:
Ligand ADP 12 x ADP
Ligand SO4 16 x SO4
1 modified residue:
Ligand MSE 156 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: P2
Unit cell:
a: 200.03Å b: 91.2Å c: 201.8Å
α: 90° β: 99.43° γ: 90°
R-values:
R R work R free
0.232 0.23 0.27
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Applications of Bacterial Degrons and Degraders - Toward Targeted Protein Degradation in Bacteria.
Izert et al. (2021)
2 more

2 mentions without citation

Heat activates the AAA+ HslUV protease by melting an axial autoinhibitory plug.
Baytshtok et al. (2021)
1 more