› 3u4m

X-ray diffraction
2Å resolution

Crystal structure of ribosomal protein tthl1 in complex with 80nt 23s rna from thermus thermophilus

Released:
DOI: 10.2210/pdb3u4m/pdb
PDB entry 3u4m coloured by chain, front view.
PDB entry 3u4m coloured by chain, side view.
PDB entry 3u4m coloured by chain, top view.
Source organism: Thermus thermophilus
Primary publication:
High-resolution crystal structure of the isolated ribosomal L1 stalk.
Tishchenko S, Gabdulkhakov A, Nevskaya N, Sarskikh A, Kostareva O, Nikonova E, Sycheva A, Moshkovskii S, Garber M, Nikonov S
Acta Crystallogr D Biol Crystallogr 68 1051-7 (2012)
PMID: 22868771

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-541439 (preferred)
Entry contents:
1 distinct polypeptide molecule
1 distinct RNA molecule
Macromolecules (2 distinct):
Large ribosomal subunit protein uL1 Chain: A
Molecule details ›
Chain: A
Length: 229 amino acids
Theoretical weight: 24.87 KDa
Source organism: Thermus thermophilus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P27150 (Residues: 1-229; Coverage: 100%)
Gene names: rpl1, rplA
Sequence domains: Ribosomal protein L1p/L10e family
Structure domains:
RNA (80-MER) Chain: B
Molecule details ›
Chain: B
Length: 80 nucleotides
Theoretical weight: 25.97 KDa
Source organism: Thermus thermophilus
Expression system: Escherichia coli BL21(DE3)
Sequence domains: Bacterial large subunit ribosomal RNA

Ligands and Environments

5 bound ligands:
Ligand SO4 2 x SO4
Ligand MLI 7 x MLI
Ligand MG 5 x MG
Ligand CL 2 x CL
Ligand NA 5 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BRUKER AXS MICROSTAR
Spacegroup: P212121
Unit cell:
a: 62.55Å b: 68.9Å c: 117.56Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.181 0.179 0.208
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 citation in other articles

Protein-RNA affinity of ribosomal protein L1 mutants does not correlate with the number of intermolecular interactions.
Tishchenko et al. (2015)
3 more

9 mentions without citation

Ensemble cryo-EM elucidates the mechanism of translation fidelity.
Loveland et al. (2017)
8 more