1feu

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spinqualitylabelsall models 1feu, resolution 2.3Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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

Overview

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.

About this Structure

1FEU is a Single protein structure of sequence from Thermus thermophilus with CD and MG as ligands. Full crystallographic information is available from OCA.

Reference

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. 2001 Jul;57(Pt 7):968-76. Epub 2001, Jun 21. PMID:11418764

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