3ZUZ

Structure of Shq1p C-terminal domain


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.50 Å
  • R-Value Free: 0.194 
  • R-Value Work: 0.171 
  • R-Value Observed: 0.172 

wwPDB Validation   3D Report Full Report


This is version 1.1 of the entry. See complete history


Literature

The H/Aca Rnp Assembly Factor Shq1 Functions as an RNA Mimic.

Walbott, H.Machado-Pinilla, R.Liger, D.Blaud, M.Rety, S.Grozdanov, P.N.Godin, K.Van Tilbeurgh, H.Varani, G.Meier, U.T.Leulliot, N.

(2011) Genes Dev 25: 2398

  • DOI: https://doi.org/10.1101/gad.176834.111
  • Primary Citation of Related Structures:  
    3ZUZ, 3ZV0

  • PubMed Abstract: 

    SHQ1 is an essential assembly factor for H/ACA ribonucleoproteins (RNPs) required for ribosome biogenesis, pre-mRNA splicing, and telomere maintenance. SHQ1 binds dyskerin/NAP57, the catalytic subunit of human H/ACA RNPs, and this interaction is modulated by mutations causing X-linked dyskeratosis congenita. We report the crystal structure of the C-terminal domain of yeast SHQ1, Shq1p, and its complex with yeast dyskerin/NAP57, Cbf5p, lacking its catalytic domain. The C-terminal domain of Shq1p interacts with the RNA-binding domain of Cbf5p and, through structural mimicry, uses the RNA-protein-binding sites to achieve a specific protein-protein interface. We propose that Shq1p operates as a Cbf5p chaperone during RNP assembly by acting as an RNA placeholder, thereby preventing Cbf5p from nonspecific RNA binding before association with an H/ACA RNA and the other core RNP proteins.


  • Organizational Affiliation

    Institut de Biochimie et de Biophysique Moléculaire et Cellulaire, Université de Paris-Sud, Orsay Cedex, France.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
PROTEIN SHQ1365Saccharomyces cerevisiae S288CMutation(s): 0 
UniProt
Find proteins for P40486 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c))
Explore P40486 
Go to UniProtKB:  P40486
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP40486
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Modified Residues  1 Unique
IDChains TypeFormula2D DiagramParent
CME
Query on CME
A
L-PEPTIDE LINKINGC5 H11 N O3 S2CYS
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.50 Å
  • R-Value Free: 0.194 
  • R-Value Work: 0.171 
  • R-Value Observed: 0.172 
  • Space Group: P 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 39.374α = 110.46
b = 50.092β = 98.85
c = 52.083γ = 97.32
Software Package:
Software NamePurpose
BUSTERrefinement
MOSFLMdata reduction
SCALAdata scaling
SHELXEphasing

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2011-11-30
    Type: Initial release
  • Version 1.1: 2019-02-27
    Changes: Data collection, Derived calculations, Experimental preparation, Other