1ZHO: The Structure Of A Ribosomal Protein L1 In Complex With Mrna

Citation:
Abstract
The RNA-binding ability of ribosomal protein L1 is of profound interest, since L1 has a dual function as a ribosomal structural protein that binds rRNA and as a translational repressor that binds its own mRNA. Here, we report the crystal structure at 2.6 A resolution of ribosomal protein L1 from the bacterium Thermus thermophilus in complex with a 38 nt fragment of L1 mRNA from Methanoccocus vannielii. The conformation of RNA-bound T.thermophilus L1 differs dramatically from that of the isolated protein. Analysis of four copies of the L1-mRNA complex in the crystal has shown that domain II of the protein does not contribute to mRNA-specific binding. A detailed comparison of the protein-RNA interactions in the L1-mRNA and L1-rRNA complexes identified amino acid residues of L1 crucial for recognition of its specific targets on the both RNAs. Incorporation of the structure of bacterial L1 into a model of the Escherichia coli ribosome revealed two additional contact regions for L1 on the 23S rRNA that were not identified in previous ribosome models.
PDB ID: 1ZHODownload
MMDB ID: 107004
PDB Deposition Date: 2005/4/26
Updated in MMDB: 2013/02
Experimental Method:
x-ray diffraction
Resolution: 2.6  Å
Source Organism:
Thermus thermophilus
Similar Structures:
Biological Unit for 1ZHO: dimeric; determined by author
Molecular Components in 1ZHO
Label Count Molecule
Protein (1 molecule)
1
50S Ribosomal Protein L1
Molecule annotation
Nucleotide(1 molecule)
1
mRNA
Molecule annotation
Chemical (1 molecule)
1
1
* Click molecule labels to explore molecular sequence information.

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