› 1m4y

X-ray diffraction
2.1Å resolution

Crystal structure of HslV from Thermotoga maritima

Released:
DOI: 10.2210/pdb1m4y/pdb
PDB entry 1m4y coloured by chain, front view.
PDB entry 1m4y coloured by chain, side view.
PDB entry 1m4y coloured by chain, top view.
Source organism: Thermotoga maritima
Primary publication:
Isolation and characterization of the prokaryotic proteasome homolog HslVU (ClpQY) from Thermotoga maritima and the crystal structure of HslV.
Song HK, Bochtler M, Azim MK, Hartmann C, Huber R, Ramachandran R
Biophys Chem 100 437-52 (2003)
PMID: 12646382

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dodecamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194559 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ATP-dependent protease subunit HslV Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 171 amino acids
Theoretical weight: 18.35 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9WYZ1 (Residues: 6-176; Coverage: 97%)
Gene names: TM_0521, hslV
Sequence domains: Proteasome subunit
Structure domains: Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1

Ligands and Environments

1 bound ligand:
Ligand NA 3 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MPG/DESY, HAMBURG BEAMLINE BW6
Spacegroup: I222
Unit cell:
a: 77.533Å b: 93.748Å c: 146.167Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.192 0.192 0.229
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Molecular machines for protein degradation.
Groll et al. (2005)
3 more

2 mentions without citation

Divergence and convergence in enzyme evolution.
Galperin et al. (2012)
1 more