1FEU: Crystal Structure Of Ribosomal Protein Tl5, One Of The Ctc Family Proteins, Complexed With A Fragment Of 5s Rrna

The crystal structure of Thermus thermophilus ribosomal protein TL5 in complex with a fragment of Escherichia coli 5S rRNA has been determined at 2.3 A resolution. The protein consists of two domains. The structure of the N-terminal domain is close to the structure of E. coli ribosomal protein L25, but the C-terminal domain represents a new fold composed of seven beta-strands connected by long loops. TL5 binds to the RNA through its N-terminal domain, whereas the C-terminal domain is not included in this interaction. Cd(2+) ions, the presence of which improved the crystal quality significantly, bind only to the protein component of the complex and stabilize the protein molecule itself and the interactions between the two molecules in the asymmetric unit of the crystal. The TL5 sequence reveals homology to the so-called general stress protein CTC. The hydrophobic cores which stabilize both TL5 domains are highly conserved in CTC proteins. Thus, all CTC proteins may fold with a topology close to that of TL5.
PDB ID: 1FEUDownload
MMDB ID: 72053
PDB Deposition Date: 2000/7/23
Updated in MMDB: 2017/10
Experimental Method:
x-ray diffraction
Resolution: 2.3  Å
Source Organism:
Thermus thermophilus
Similar Structures:
Biological Unit for 1FEU: trimeric; determined by author
Molecular Components in 1FEU
Label Count Molecule
Protein (1 molecule)
50S Ribosomal Protein L25
Molecule annotation
Nucleotides(2 molecules)
19 NT Fragment of 5S rRNA
Molecule annotation
21 NT Fragment of 5S rRNA
Molecule annotation
Chemicals (11 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB