1BXY

CRYSTAL STRUCTURE OF RIBOSOMAL PROTEIN L30 FROM THERMUS THERMOPHILUS AT 1.9 A RESOLUTION: CONFORMATIONAL FLEXIBILITY OF THE MOLECULE.


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.90 Å
  • R-Value Free: 0.253 
  • R-Value Work: 0.203 
  • R-Value Observed: 0.203 

wwPDB Validation   3D Report Full Report


This is version 1.5 of the entry. See complete history


Literature

Structure of ribosomal protein L30 from Thermus thermophilus at 1.9 A resolution: conformational flexibility of the molecule.

Fedorov, R.Nevskaya, N.Khairullina, A.Tishchenko, S.Mikhailov, A.Garber, M.Nikonov, S.

(1999) Acta Crystallogr D Biol Crystallogr 55: 1827-1833

  • DOI: https://doi.org/10.1107/s0907444999010227
  • Primary Citation of Related Structures:  
    1BXY

  • PubMed Abstract: 

    The crystal structure of ribosomal protein L30 from the extreme thermophilic bacterium Thermus thermophilus has been determined at 1. 9 A resolution. The crystals are trigonal and belong to space group P3(2)21, with unit-cell parameters a = b = 63.5, c = 77.8 A, alpha = beta = 90, gamma = 120 degrees and two molecules per asymmetric unit. The structure was solved by the molecular-replacement method with AMoRe and refined with X-PLOR to an R value of 20.3% and an R(free) of 25.3% in the resolution range 8-1.9 A. Detailed analyses of the structures of the two molecules in the asymmetric unit and comparison of T. thermophilus L30 structure with the structure of homologous L30 from Bacillus stearothermophilus reveal two flexible regions at opposite ends of the rather elongated molecule. Such flexibility could be important for the protein fitting in the ribosome. A comparison with B. stearothermophilus L30 shows a higher number of salt bridges and unbound positively charged residues and an increased accessible hydrophobic area on the surface of T. thermophilus L30. This could contribute to the stability of both the extreme thermophile protein and the ribosome as a whole.


  • Organizational Affiliation

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


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
PROTEIN (RIBOSOMAL PROTEIN L30)
A, B
60Thermus thermophilusMutation(s): 0 
Gene Names: RPL30
UniProt
Find proteins for P74909 (Thermus thermophilus)
Explore P74909 
Go to UniProtKB:  P74909
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP74909
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.90 Å
  • R-Value Free: 0.253 
  • R-Value Work: 0.203 
  • R-Value Observed: 0.203 
  • Space Group: P 32 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 63.5α = 90
b = 63.5β = 90
c = 77.8γ = 120
Software Package:
Software NamePurpose
AMoREphasing
X-PLORrefinement
MOSFLMdata reduction
SCALEPACKdata scaling

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1998-10-14
    Type: Initial release
  • Version 1.1: 2008-04-27
    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: 2019-12-11
    Changes: Advisory, Derived calculations
  • Version 1.5: 2024-02-07
    Changes: Data collection, Database references