› 1g4a

X-ray diffraction
3Å resolution

CRYSTAL STRUCTURES OF THE HSLVU PEPTIDASE-ATPASE COMPLEX REVEAL AN ATP-DEPENDENT PROTEOLYSIS MECHANISM

Released:
DOI: 10.2210/pdb1g4a/pdb
PDB entry 1g4a coloured by chain, front view.
PDB entry 1g4a coloured by chain, side view.
PDB entry 1g4a coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Crystal structures of the HslVU peptidase-ATPase complex reveal an ATP-dependent proteolysis mechanism.
Wang J, Song JJ, Franklin MC, Kamtekar S, Im YJ, Rho SH, Seong IS, Lee CS, Chung CH, Eom SH
Structure 9 177-84 (2001)
PMID: 11250202

Function and Biology Details

Reaction catalysed: 
ATP-dependent cleavage of peptide bonds with broad specificity.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
hetero octadecamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141353 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
ATP-dependent protease ATPase subunit HslU Chains: E, F
Molecule details ›
Chains: E, F
Length: 443 amino acids
Theoretical weight: 49.66 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A6H5 (Residues: 1-443; Coverage: 100%)
Gene names: JW3902, b3931, hslU, htpI
Sequence domains:
Structure domains:
ATP-dependent protease subunit HslV Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 175 amino acids
Theoretical weight: 18.99 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A7B8 (Residues: 2-176; Coverage: 99%)
Gene names: JW3903, b3932, hslV, htpO, yiiC
Sequence domains: Proteasome subunit
Structure domains: Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1

Ligands and Environments

1 bound ligand:
Ligand DAT 2 x DAT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.3
Spacegroup: P321
Unit cell:
a: 169.995Å b: 169.995Å c: 161.317Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.257 0.257 0.294
Expression system: Escherichia coli

Quick links

Citations

48 review citations

AAA+ proteins: have engine, will work.
Hanson et al. (2005)
47 more

3 mentions without citation

The AAA+ superfamily of functionally diverse proteins.
Snider et al. (2008)
2 more