5IZW

Crystal structure of RNA editing specific factor of designer PLS-type PPR-9R protein


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.74 Å
  • R-Value Free: 0.208 
  • 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

MORF9 increases the RNA-binding activity of PLS-type pentatricopeptide repeat protein in plastid RNA editing

Yan, J.Zhang, Q.Guan, Z.Wang, Q.Li, L.Ruan, F.Lin, R.Zou, T.Yin, P.

(2017) Nat Plants 3: 17037-17037

  • DOI: https://doi.org/10.1038/nplants.2017.37
  • Primary Citation of Related Structures:  
    5GI0, 5IWW, 5IZW

  • PubMed Abstract: 

    RNA editing is a post-transcriptional process that modifies the genetic information on RNA molecules. In flowering plants, RNA editing usually alters cytidine to uridine in plastids and mitochondria. The PLS-type pentatricopeptide repeat (PPR) protein and the multiple organellar RNA editing factor (MORF, also known as RNA editing factor interacting protein (RIP)) are two types of key trans-acting factors involved in this process. However, how they cooperate with one another remains unclear. Here, we have characterized the interactions between a designer PLS-type PPR protein (PLS) 3 PPR and MORF9, and found that RNA-binding activity of (PLS) 3 PPR is drastically increased on MORF9 binding. We also determined the crystal structures of (PLS) 3 PPR, MORF9 and the (PLS) 3 PPR-MORF9 complex. MORF9 binding induces significant compressed conformational changes of (PLS) 3 PPR, revealing the molecular mechanisms by which MORF9-bound (PLS) 3 PPR has increased RNA-binding activity. Similarly, increased RNA-binding activity is observed for the natural PLS-type PPR protein, LPA66, in the presence of MORF9. These findings significantly expand our understanding of MORF function in plant organellar RNA editing.


  • Organizational Affiliation

    National Key Laboratory of Crop Genetic Improvement and National Centre of Plant Gene Research, Huazhong Agricultural University, Wuhan 430070, China.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
PLS9-PPR
A, B
101unidentifiedMutation(s): 0 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.74 Å
  • R-Value Free: 0.208 
  • R-Value Work: 0.175 
  • R-Value Observed: 0.177 
  • Space Group: P 41
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 67.412α = 90
b = 67.412β = 90
c = 56.752γ = 90
Software Package:
Software NamePurpose
PHENIXrefinement
HKL-3000data collection
HKL-3000data scaling
SHELXDEphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2017-03-29
    Type: Initial release
  • Version 1.1: 2017-09-27
    Changes: Data collection
  • Version 1.2: 2017-11-15
    Changes: Database references
  • Version 1.3: 2024-03-20
    Changes: Data collection, Database references