1CJS

CRYSTAL STRUCTURE OF RIBOSOMAL PROTEIN L1 FROM METHANOCOCCUS JANNASCHII


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.30 Å
  • R-Value Free: 0.271 
  • R-Value Work: 0.203 
  • R-Value Observed: 0.203 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history


Literature

Archaeal ribosomal protein L1: the structure provides new insights into RNA binding of the L1 protein family.

Nevskaya, N.Tischenko, S.Fedorov, R.Al-Karadaghi, S.Liljas, A.Kraft, A.Piendl, W.Garber, M.Nikonov, S.

(2000) Structure 8: 363-371

  • DOI: https://doi.org/10.1016/s0969-2126(00)00116-7
  • Primary Citation of Related Structures:  
    1CJS

  • PubMed Abstract: 

    L1 is an important primary rRNA-binding protein, as well as a translational repressor that binds mRNA. It was shown that L1 proteins from some bacteria and archaea are functionally interchangeable within the ribosome and in the repression of translation. The crystal structure of bacterial L1 from Thermus thermophilus (TthL1) has previously been determined.


  • Organizational Affiliation

    Institute of Protein Research, Russian Academy of Sciences, Pushchino, 142292, Moscow Region, Russia.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
50S RIBOSOMAL PROTEIN L1P219Methanocaldococcus jannaschiiMutation(s): 0 
Gene Names: RPLA
UniProt
Find proteins for P54050 (Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440))
Explore P54050 
Go to UniProtKB:  P54050
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP54050
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.30 Å
  • R-Value Free: 0.271 
  • R-Value Work: 0.203 
  • R-Value Observed: 0.203 
  • Space Group: P 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 34.407α = 83.03
b = 39.91β = 80.25
c = 55.634γ = 74.68
Software Package:
Software NamePurpose
X-PLORmodel building
CCP4model building
Omodel building
X-PLORrefinement
DENZOdata reduction
SCALEPACKdata scaling
X-PLORphasing
CCP4phasing

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2000-05-31
    Type: Initial release
  • Version 1.1: 2008-04-26
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2018-03-07
    Changes: Data collection
  • Version 1.4: 2023-12-27
    Changes: Data collection, Database references