› 2ghj

X-ray diffraction
2.9Å resolution

Crystal structure of folded and partially unfolded forms of Aquifex aeolicus ribosomal protein L20

Released:
DOI: 10.2210/pdb2ghj/pdb
PDB entry 2ghj coloured by chain, front view.
PDB entry 2ghj coloured by chain, side view.
PDB entry 2ghj coloured by chain, top view.
Source organism: Aquifex aeolicus
Primary publication:
Coexistence of two protein folding states in the crystal structure of ribosomal protein L20.
Timsit Y, Allemand F, Chiaruttini C, Springer M
EMBO Rep 7 1013-8 (2006)
PMID: 16977336

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-130442 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Large ribosomal subunit protein bL20 Chains: A, B, D, E
Molecule details ›
Chains: A, B, D, E
Length: 118 amino acids
Theoretical weight: 14.18 KDa
Source organism: Aquifex aeolicus
Expression system: Escherichia coli
UniProt:
  • Canonical: O67086 (Residues: 1-118; Coverage: 100%)
Gene names: aq_952, rplT
Sequence domains: Ribosomal protein L20
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand SO4 6 x SO4
1 modified residue:
Ligand MSE 12 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM30A
Spacegroup: P1
Unit cell:
a: 44.914Å b: 45.217Å c: 67.06Å
α: 104.06° β: 106.2° γ: 97.76°
R-values:
R R work R free
0.22 0.22 0.292
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Intrinsically disordered chaperones in plants and animals.
Tompa et al. (2010)
7 more

3 mentions without citation

Coexistence of two protein folding states in the crystal structure of ribosomal protein L20.
Timsit et al. (2006)
2 more