6BUA

Drosophila Dicer-2 apo homology model (helicase, Platform-PAZ, RNaseIII domains)


Experimental Data Snapshot

  • Method: ELECTRON MICROSCOPY
  • Resolution: 7.10 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

wwPDB Validation   3D Report Full Report


This is version 1.6 of the entry. See complete history


Literature

Dicer uses distinct modules for recognizing dsRNA termini.

Sinha, N.K.Iwasa, J.Shen, P.S.Bass, B.L.

(2018) Science 359: 329-334

  • DOI: https://doi.org/10.1126/science.aaq0921
  • Primary Citation of Related Structures:  
    6BU9, 6BUA

  • PubMed Abstract: 

    Invertebrates rely on Dicer to cleave viral double-stranded RNA (dsRNA), and Drosophila Dicer-2 distinguishes dsRNA substrates by their termini. Blunt termini promote processive cleavage, while 3' overhanging termini are cleaved distributively. To understand this discrimination, we used cryo-electron microscopy to solve structures of Drosophila Dicer-2 alone and in complex with blunt dsRNA. Whereas the Platform-PAZ domains have been considered the only Dicer domains that bind dsRNA termini, unexpectedly, we found that the helicase domain is required for binding blunt, but not 3' overhanging, termini. We further showed that blunt dsRNA is locally unwound and threaded through the helicase domain in an adenosine triphosphate-dependent manner. Our studies reveal a previously unrecognized mechanism for optimizing antiviral defense and set the stage for the discovery of helicase-dependent functions in other Dicers.


  • Organizational Affiliation

    Department of Biochemistry, University of Utah, Salt Lake City, UT 84112, USA. bbass@biochem.utah.edu peter.shen@biochem.utah.edu.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Dicer-2, isoform A1,724Drosophila melanogasterMutation(s): 0 
Gene Names: Dcr-2Dcr-2-RACG6493Dmel_CG6493
EC: 3.1.26.3 (PDB Primary Data), 3.6.1.3 (PDB Primary Data)
UniProt
Find proteins for A1ZAW0 (Drosophila melanogaster)
Explore A1ZAW0 
Go to UniProtKB:  A1ZAW0
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA1ZAW0
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: ELECTRON MICROSCOPY
  • Resolution: 7.10 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

Structure Validation

View Full Validation Report



Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)United StatesR01GM121706

Revision History  (Full details and data files)

  • Version 1.0: 2017-12-27
    Type: Initial release
  • Version 1.1: 2018-01-03
    Changes: Database references
  • Version 1.2: 2018-01-17
    Changes: Author supporting evidence
  • Version 1.3: 2018-01-31
    Changes: Database references
  • Version 1.4: 2019-11-20
    Changes: Database references
  • Version 1.5: 2020-01-08
    Changes: Author supporting evidence
  • Version 1.6: 2024-03-13
    Changes: Data collection, Database references