2FTC

Structural Model for the Large Subunit of the Mammalian Mitochondrial Ribosome


Experimental Data Snapshot

  • Method: ELECTRON MICROSCOPY
  • Resolution: 12.1 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

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This is version 1.3 of the entry. See complete history


Literature

A Structural Model for the Large Subunit of the Mammalian Mitochondrial Ribosome

Mears, J.A.Sharma, M.R.Gutell, R.R.McCook, A.S.Richardson, P.E.Caulfield, T.R.Agrawal, R.K.Harvey, S.C.

(2006) J Mol Biol 358: 193-212

  • DOI: https://doi.org/10.1016/j.jmb.2006.01.094
  • Primary Citation of Related Structures:  
    2FTC

  • PubMed Abstract: 

    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.


  • Organizational Affiliation

    Department of Biology, Georgia Institute of Technology, Atlanta, GA 30332, USA.


Macromolecules

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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Mitochondrial ribosomal protein L1B [auth A]189Bos taurusMutation(s): 0 
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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
mitochondrial ribosomal protein L2C [auth B]136Bos taurusMutation(s): 0 
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Entity ID: 4
MoleculeChains Sequence LengthOrganismDetailsImage
Mitochondrial 39S ribosomal protein L3D [auth C]211Bos taurusMutation(s): 0 
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Entity ID: 5
MoleculeChains Sequence LengthOrganismDetailsImage
mitochondrial ribosomal protein L4 isoform aE [auth D]175Bos taurusMutation(s): 0 
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Entity ID: 6
MoleculeChains Sequence LengthOrganismDetailsImage
39S ribosomal protein L12, mitochondrialF [auth E],
G [auth F]
137Bos taurusMutation(s): 0 
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Entity ID: 7
MoleculeChains Sequence LengthOrganismDetailsImage
39S ribosomal protein L11, mitochondrialH [auth G]145Bos taurusMutation(s): 0 
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Entity ID: 8
MoleculeChains Sequence LengthOrganismDetailsImage
39S ribosomal protein L13, mitochondrialI [auth H]148Bos taurusMutation(s): 0 
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Entity ID: 9
MoleculeChains Sequence LengthOrganismDetailsImage
Mitochondrial ribosomal protein L16J [auth I]118Bos taurusMutation(s): 0 
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Entity ID: 10
MoleculeChains Sequence LengthOrganismDetailsImage
Mitochondrial ribosomal protein L17K [auth J]116Bos taurusMutation(s): 0 
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Entity ID: 11
MoleculeChains Sequence LengthOrganismDetailsImage
39S ribosomal protein L19, mitochondrialL [auth K]98Bos taurusMutation(s): 0 
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Entity ID: 12
MoleculeChains Sequence LengthOrganismDetailsImage
MRPL20 proteinM [auth L]118Bos taurusMutation(s): 0 
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Entity ID: 13
MoleculeChains Sequence LengthOrganismDetailsImage
mitochondrial ribosomal protein L22 isoform aN [auth M]110Bos taurusMutation(s): 0 
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Entity ID: 14
MoleculeChains Sequence LengthOrganismDetailsImage
mitochondrial ribosomal protein L24O [auth N]96Bos taurusMutation(s): 0 
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Entity ID: 15
MoleculeChains Sequence LengthOrganismDetailsImage
Mitochondrial 39S ribosomal protein L27P [auth O]69Bos taurusMutation(s): 0 
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Entity ID: 16
MoleculeChains Sequence LengthOrganismDetailsImage
mitochondrial ribosomal protein L33 isoform aQ [auth P]52Bos taurusMutation(s): 0 
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Entity ID: 17
MoleculeChains Sequence LengthOrganismDetailsImage
39S ribosomal protein L34, mitochondrialR [auth Q]38Bos taurusMutation(s): 0 
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Entity ID: 1
MoleculeChains LengthOrganismImage
Mitochondrial 16S ribosomal RNAA [auth R]1,568Bos taurus
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Experimental Data & Validation

Experimental Data

  • Method: ELECTRON MICROSCOPY
  • Resolution: 12.1 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2006-04-11
    Type: Initial release
  • Version 1.1: 2008-05-01
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2024-02-14
    Changes: Data collection, Database references, Refinement description