4C4A

Crystal structure of mouse protein arginine methyltransferase 7 in complex with SAH

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.70 Å
  • R-Value Free: 0.190 
  • R-Value Work: 0.160 
  • R-Value Observed: 0.161 

Starting Model: experimental
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This is version 1.4 of the entry. See complete history. 


Literature

Structural Insight Into Arginine Methylation by the Mouse Protein Arginine Methyltransferase 7: A Zinc Finger Freezes the Mimic of the Dimeric State Into a Single Active Site.

Cura, V., Troffer-Charlier, N., Wurtz, J.M., Bonnefond, L., Cavarelli, J.

(2014) Acta Crystallogr D Biol Crystallogr 70: 2401

  • DOI: https://doi.org/10.1107/S1399004714014278
  • Primary Citation of Related Structures:  
    4C4A

  • PubMed Abstract: 

    Protein arginine methyltransferase 7 (PRMT7) is a type III arginine methyltransferase which has been implicated in several biological processes such as transcriptional regulation, DNA damage repair, RNA splicing, cell differentiation and metastasis. PRMT7 is a unique but less characterized member of the family of PRMTs. The crystal structure of full-length PRMT7 from Mus musculus refined at 1.7 Å resolution is described. The PRMT7 structure is composed of two catalytic modules in tandem forming a pseudo-dimer and contains only one AdoHcy molecule bound to the N-terminal module. The high-resolution crystal structure presented here revealed several structural features showing that the second active site is frozen in an inactive state by a conserved zinc finger located at the junction between the two PRMT modules and by the collapse of two degenerated AdoMet-binding loops.

    • Organizational Affiliation: 

    Département de Biologie Structurale Intégrative, Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), Université de Strasbourg, CNRS UMR7104, INSERM U596, 1 Rue Laurent Fries, F-67404 Illkirch, France.


Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
PROTEIN ARGININE N-METHYLTRANSFERASE 7692Mus musculusMutation(s): 0 
EC: 2.1.1 (PDB Primary Data), 2.1.1.125 (PDB Primary Data), 2.1.1.126 (PDB Primary Data), 2.1.1.321 (UniProt)
UniProt & NIH Common Fund Data Resources
Find proteins for Q922X9 (Mus musculus)
Explore Q922X9 
Go to UniProtKB:  Q922X9
IMPC:  MGI:2384879
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ922X9
Sequence Annotations
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  • Reference Sequence
Small Molecules
Binding Affinity Annotations 
IDSourceBinding Affinity
SAH BindingDB:  4C4A IC50: min: 110, max: 5.00e+4 (nM) from 2 assay(s)
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.70 Å
  • R-Value Free: 0.190 
  • R-Value Work: 0.160 
  • R-Value Observed: 0.161 
  • Space Group: P 43 21 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 97.322α = 90
b = 97.322β = 90
c = 168.754γ = 90
Software Package:
Software NamePurpose
PHENIXrefinement
XDSdata reduction
Aimlessdata scaling
PHASERphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2014-07-02
    Type: Initial release
  • Version 1.1: 2014-09-10
    Changes: Database references, Structure summary
  • Version 1.2: 2014-09-24
    Changes: Database references
  • Version 1.3: 2017-08-23
    Changes: Data collection
  • Version 1.4: 2024-05-01
    Changes: Data collection, Database references, Derived calculations, Other, Refinement description