1FEU

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

Summary for 1FEU

• Entry DOI: 10.2210/pdb1feu/pdb
• Descriptor: 19 NT FRAGMENT OF 5S RRNA, 21 NT FRAGMENT OF 5S RRNA, 50S RIBOSOMAL PROTEIN L25, ... (6 entities in total)
• Functional Keywords: general stress protein ctc, 5s rrna-protein complex, cadmium ions, ribosome
• Biological source: Thermus thermophilus
• Total number of polymer chains: 6
• Total formula weight: 74373.42

Authors

Fedorov, R.V.,Meshcheryakov, V.A.,Gongadze, G.M.,Fomenkova, N.P.,Nevskaya, N.A.,Selmer, M.,Laurberg, M.,Kristensen, O.,Al-Karadaghi, S.,Liljas, A.,Garber, M.B.,Nikonov, S.V. (deposition date: 2000-07-23, release date: 2001-06-25, Last modification date: 2024-02-07)

Primary citation

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.
Structure of ribosomal protein TL5 complexed with RNA provides new insights into the CTC family of stress proteins.
Acta Crystallogr.,Sect.D, 57:968-976, 2001

PubMed Abstract: 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.

PubMed: 11418764
DOI: 10.1107/S0907444901006291

Experimental method

X-RAY DIFFRACTION (2.3 Å)