› 1feu

X-ray diffraction
2.3Å resolution

CRYSTAL STRUCTURE OF RIBOSOMAL PROTEIN TL5, ONE OF THE CTC FAMILY PROTEINS, COMPLEXED WITH A FRAGMENT OF 5S RRNA.

Released:
DOI: 10.2210/pdb1feu/pdb
PDB entry 1feu coloured by chain, front view.
PDB entry 1feu coloured by chain, side view.
PDB entry 1feu coloured by chain, top view.
Source organism: Thermus thermophilus
Primary publication:
Structure of ribosomal protein TL5 complexed with RNA provides new insights into the CTC family of stress proteins.
Fedorov R, Meshcheryakov V, Gongadze G, Fomenkova N, Nevskaya N, Selmer M, Laurberg M, Kristensen O, Al-Karadaghi S, Liljas A, Garber M, Nikonov S
Acta Crystallogr D Biol Crystallogr 57 968-76 (2001)
PMID: 11418764

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-157579 (preferred)
Entry contents:
1 distinct polypeptide molecule
2 distinct RNA molecules
Macromolecules (3 distinct):
Large ribosomal subunit protein bL25 Chains: A, D
Molecule details ›
Chains: A, D
Length: 206 amino acids
Theoretical weight: 23.25 KDa
Source organism: Thermus thermophilus
Expression system: Escherichia coli
UniProt:
  • Canonical: P56930 (Residues: 1-206; Coverage: 100%)
Gene names: rpl25, rplY, rptL5
Sequence domains:
Structure domains:
19 NT FRAGMENT OF 5S RRNA Chains: B, E
Molecule details ›
Chains: B, E
Length: 19 nucleotides
Theoretical weight: 6.21 KDa
Source organism: Thermus thermophilus
Expression system: Not provided
21 NT FRAGMENT OF 5S RRNA Chains: C, F
Molecule details ›
Chains: C, F
Length: 21 nucleotides
Theoretical weight: 6.79 KDa
Source organism: Thermus thermophilus
Expression system: Not provided

Ligands and Environments

2 bound ligands:
Ligand MG 17 x MG
Ligand CD 13 x CD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I711
Spacegroup: P3112
Unit cell:
a: 109.904Å b: 109.904Å c: 137.511Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.208 0.208 0.245
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

6 review citations

Cyclic di-AMP: another second messenger enters the fray.
Corrigan et al. (2013)
5 more

11 mentions without citation

DARS-RNP and QUASI-RNP: new statistical potentials for protein-RNA docking.
Tuszynska et al. (2011)
10 more