1NRJ

Signal Recognition Particle Receptor Beta-Subunit in Complex with the SRX Domain from the Alpha-Subunit

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.70 Å
  • R-Value Free: 0.229 
  • R-Value Work: 0.194 
  • R-Value Observed: 0.196 

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This is version 1.4 of the entry. See complete history. 


Literature

Structural Basis for the Function of the beta Subunit of the Eukaryotic Signal Recognition Particle Receptor

Schwartz, T., Blobel, G.

(2003) Cell 112: 793-803

  • DOI: https://doi.org/10.1016/s0092-8674(03)00161-2
  • Primary Citation of Related Structures:  
    1NRJ

  • PubMed Abstract: 

    Protein translocation across and insertion into membranes is a process essential to all life forms. In higher eukaryotes, this process is initiated by targeting the translating ribosome to the endoplasmic reticulum via the signal recognition particle (SRP) and its membrane-associated heterodimeric receptor (SR). This targeting step is regulated by three G proteins, SRP54, SR alpha, and SR beta, which act in concert. Little is known about the regulatory role of SR beta. Here, we present the 1.7 A crystal structure of the SR beta-GTP subunit in complex with the interaction domain of SR alpha. Strikingly, the binding interface overlaps largely with the switch 1 region of SR beta. This finding, together with additional biochemical data, shows that the eukaryotic SR is a conditional and not an obligate heterodimer. The results suggest that the GTP/GDP switch cycle of SR beta functions as a regulatory switch for the receptor dimerization. We discuss the implications for the translocation pathway.

    • Organizational Affiliation: 

    Howard Hughes Medical Institute, Laboratory of Cell Biology, The Rockefeller University, 1230 York Avenue, New York, NY 10021, USA.


Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Signal recognition particle receptor alpha subunit homolog158Saccharomyces cerevisiaeMutation(s): 0 
Gene Names: SRP101
Membrane Entity: Yes 
UniProt
Find proteins for P32916 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c))
Explore P32916 
Go to UniProtKB:  P32916
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP32916
Sequence Annotations
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  • Reference Sequence
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Signal recognition particle receptor beta subunit218Saccharomyces cerevisiaeMutation(s): 0 
Gene Names: SRP102
Membrane Entity: Yes 
UniProt
Find proteins for P36057 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c))
Explore P36057 
Go to UniProtKB:  P36057
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP36057
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Binding Affinity Annotations 
IDSourceBinding Affinity
GTP Binding MOAD:  1NRJ Kd: 38 (nM) from 1 assay(s)
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.70 Å
  • R-Value Free: 0.229 
  • R-Value Work: 0.194 
  • R-Value Observed: 0.196 
  • Space Group: P 21 21 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 78.2α = 90
b = 123.7β = 90
c = 48.8γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
HKL-2000data reduction
SCALEPACKdata scaling
SnBphasing
SHARPphasing
DMphasing

Structure Validation

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Entry History 

Deposition Data

  • Released Date: 2003-03-25 
    • Deposition Author(s): Schwartz, T.

Revision History  (Full details and data files)

  • Version 1.0: 2003-03-25
    Type: Initial release
  • Version 1.1: 2008-04-29
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2017-10-11
    Changes: Refinement description
  • Version 1.4: 2024-02-14
    Changes: Data collection, Database references, Derived calculations