2ftc
Structural Model for the Large Subunit of the Mammalian Mitochondrial Ribosome
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OverviewOverview
Protein translation is essential for all forms of life and is conducted by, a macromolecular complex, the ribosome. Evolutionary changes in protein, and RNA sequences can affect the 3D organization of structural features in, ribosomes in different species. The most dramatic changes occur in animal, mitochondria, whose genomes have been reduced and altered significantly., The RNA component of the mitochondrial ribosome (mitoribosome) is reduced, in size, with a compensatory increase in protein content. Until recently, it was unclear how these changes affect the 3D structure of the, mitoribosome. Here, we present a structural model of the large subunit of, the mammalian mitoribosome developed by combining molecular modeling, techniques with cryo-electron microscopic data at 12.1A resolution. The, model contains 93% of the mitochondrial rRNA sequence and 16 mitochondrial, ribosomal proteins in the large subunit of the mitoribosome. Despite the, smaller mitochondrial rRNA, the spatial positions of RNA domains known to, be involved directly in protein synthesis are essentially the same as in, bacterial and archaeal ribosomes. However, the dramatic reduction in rRNA, content necessitates evolution of unique structural features to maintain, connectivity between RNA domains. The smaller rRNA sequence also limits, the likelihood of tRNA binding at the E-site of the mitoribosome, and, correlates with the reduced size of D-loops and T-loops in some animal, mitochondrial tRNAs, suggesting co-evolution of mitochondrial rRNA and, tRNA structures.
About this StructureAbout this Structure
2FTC is a Protein complex structure of sequences from Bos taurus. Full crystallographic information is available from OCA.
ReferenceReference
A structural model for the large subunit of the mammalian mitochondrial ribosome., Mears JA, Sharma MR, Gutell RR, McCook AS, Richardson PE, Caulfield TR, Agrawal RK, Harvey SC, J Mol Biol. 2006 Apr 21;358(1):193-212. Epub 2006 Feb 10. PMID:16510155
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