2QUX

PP7 coat protein dimer in complex with RNA hairpin


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.44 Å
  • R-Value Free: 0.236 
  • R-Value Work: 0.175 
  • R-Value Observed: 0.177 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Structural basis for the coevolution of a viral RNA-protein complex.

Chao, J.A.Patskovsky, Y.Almo, S.C.Singer, R.H.

(2008) Nat Struct Mol Biol 15: 103-105

  • DOI: https://doi.org/10.1038/nsmb1327
  • Primary Citation of Related Structures:  
    2QUD, 2QUX

  • PubMed Abstract: 

    The cocrystal structure of the PP7 bacteriophage coat protein in complex with its translational operator identifies a distinct mode of sequence-specific RNA recognition when compared to the well-characterized MS2 coat protein-RNA complex. The structure reveals the molecular basis of the PP7 coat protein's ability to selectively bind its cognate RNA, and it demonstrates that the conserved beta-sheet surface is a flexible architecture that can evolve to recognize diverse RNA hairpins.


  • Organizational Affiliation

    Department of Anatomy, Albert Einstein College of Medicine, 1300 Morris Park Ave, Bronx, New York 10461, USA.


Macromolecules

Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Coat protein125Pseudomonas phage PP7Mutation(s): 0 
Gene Names: PP7 coat protein
UniProt
Find proteins for P03630 (Pseudomonas phage PP7)
Explore P03630 
Go to UniProtKB:  P03630
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP03630
Sequence Annotations
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  • Reference Sequence

Find similar nucleic acids by:  Sequence   |   3D Structure  

Entity ID: 1
MoleculeChains LengthOrganismImage
RNA (25-MER)25N/A
Sequence Annotations
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  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
GOL
Query on GOL

Download Ideal Coordinates CCD File 
AA [auth D]
BA [auth E]
CA [auth G]
DA [auth H]
EA [auth J]
AA [auth D],
BA [auth E],
CA [auth G],
DA [auth H],
EA [auth J],
FA [auth J],
GA [auth K],
S [auth I],
T [auth L],
U [auth R],
V [auth A],
W [auth A],
X [auth B],
Y [auth B],
Z [auth D]
GLYCEROL
C3 H8 O3
PEDCQBHIVMGVHV-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.44 Å
  • R-Value Free: 0.236 
  • R-Value Work: 0.175 
  • R-Value Observed: 0.177 
  • Space Group: C 1 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 174.97α = 90
b = 145.388β = 122.94
c = 109.655γ = 90
Software Package:
Software NamePurpose
PHASERphasing
REFMACrefinement
HKL-2000data reduction
HKL-2000data scaling

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

  • Released Date: 2007-12-18 
  • Deposition Author(s): Chao, J.A.

Revision History  (Full details and data files)

  • Version 1.0: 2007-12-18
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Non-polymer description, Version format compliance
  • Version 1.2: 2017-08-02
    Changes: Refinement description, Source and taxonomy
  • Version 1.3: 2023-08-30
    Changes: Data collection, Database references, Derived calculations, Refinement description