› 2ku2

Solution NMR

Dynamic Regulation of Archaeal Proteasome Gate Opening as Studied by TROSY-NMR

Released:
DOI: 10.2210/pdb2ku2/pdb
PDB entry 2ku2 coloured by chain, ensemble of 50 models, front view.
PDB entry 2ku2 coloured by chain, ensemble of 50 models, side view.
PDB entry 2ku2 coloured by chain, ensemble of 50 models, top view.
Source organism: Thermoplasma acidophilum
Primary publication:
Dynamic regulation of archaeal proteasome gate opening as studied by TROSY NMR.
Religa TL, Sprangers R, Kay LE
Science 328 98-102 (2010)
PMID: 20360109

Function and Biology Details

Reaction catalysed: 
Cleavage of peptide bonds with very broad specificity.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo heptamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150394 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Proteasome subunit alpha Chains: A, B, C, D, E, F, G
Molecule details ›
Chains: A, B, C, D, E, F, G
Length: 237 amino acids
Theoretical weight: 25.98 KDa
Source organism: Thermoplasma acidophilum
Expression system: Escherichia coli
UniProt:
  • Canonical: P25156 (Residues: 1-233; Coverage: 100%)
Gene names: Ta1288, psmA
Sequence domains:
Structure domains: Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing
Expression system: Escherichia coli

Quick links

Citations

42 review citations

An introduction to NMR-based approaches for measuring protein dynamics.
Kleckner et al. (2011)
41 more

1 mention without citation

Multi-core CPU or GPU-accelerated Multiscale Modeling for Biomolecular Complexes.
Liao et al. (2013)