1YSH

Localization and dynamic behavior of ribosomal protein L30e

Experimental Data Snapshot

  • Method: ELECTRON MICROSCOPY
  • Resolution: 9.50 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

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This is version 1.3 of the entry. See complete history. 


Literature

Localization and dynamic behavior of ribosomal protein L30e

Halic, M., Becker, T., Frank, J., Spahn, C.M., Beckmann, R.

(2005) Nat Struct Mol Biol 12: 467-468

  • DOI: https://doi.org/10.1038/nsmb933
  • Primary Citation of Related Structures:  
    1YSH

  • PubMed Abstract: 

    The ribosomal protein L30e is an indispensable component of the eukaryotic 80S ribosome, where it is part of the large (60S) ribosomal subunit. Here, we determined the localization of L30e in the cryo-EM map of the 80S wheat germ (wg) ribosome at a resolution of 9.5 A. L30e is part of the interface between large and small subunits, where it dynamically participates in the formation of the two intersubunit bridges eB9 and B4.

    • Organizational Affiliation: 

    Institute of Biochemistry, Charité, University Medical School Berlin, Monbijoustrasse 2, 10117 Berlin, Germany.


Macromolecules

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Entity ID: 4
MoleculeChains Sequence LengthOrganismDetailsImage
ribosomal protein L30D [auth C]104Triticum aestivumMutation(s): 0 
UniProt
Find proteins for Q5I7K9 (Triticum aestivum)
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Go to UniProtKB:  Q5I7K9
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UniProt GroupQ5I7K9
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Entity ID: 5
MoleculeChains Sequence LengthOrganismDetailsImage
ribosomal protein L37aE [auth D]73Oryza sativaMutation(s): 0 
UniProt
Find proteins for P0DKK1 (Oryza sativa subsp. japonica)
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UniProt GroupP0DKK1
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Entity ID: 6
MoleculeChains Sequence LengthOrganismDetailsImage
40S RIBOSOMAL PROTEIN S13F [auth E]84Oryza sativaMutation(s): 0 
UniProt
Find proteins for Q69UI2 (Oryza sativa subsp. japonica)
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Go to UniProtKB:  Q69UI2
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UniProt GroupQ69UI2
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Entity ID: 1
MoleculeChains LengthOrganismImage
RNA (28-MER)28synthetic construct
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Entity ID: 2
MoleculeChains LengthOrganismImage
RNA (34-MER)B [auth F]34synthetic construct
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Entity ID: 3
MoleculeChains LengthOrganismImage
RNA (101-MER)C [auth B]101synthetic construct
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: ELECTRON MICROSCOPY
  • Resolution: 9.50 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 
EM Software:
TaskSoftware PackageVersion
RECONSTRUCTIONSPIDER

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2005-07-05
    Type: Initial release
  • Version 1.1: 2008-04-30
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2019-12-18
    Changes: Data collection, Database references, Source and taxonomy