5G2Y

Structure a of Group II Intron Complexed with its Reverse Transcriptase


Experimental Data Snapshot

  • Method: ELECTRON MICROSCOPY
  • Resolution: 4.50 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Structure of a Group II Intron in Complex with its Reverse Transcriptase.

Qu, G.Kaushal, P.S.Wang, J.Shigematsu, H.Piazza, C.L.Agrawal, R.K.Belfort, M.Wang, H.

(2016) Nat Struct Mol Biol 23: 549

  • DOI: https://doi.org/10.1038/nsmb.3220
  • Primary Citation of Related Structures:  
    5G2X, 5G2Y

  • PubMed Abstract: 

    Bacterial group II introns are large catalytic RNAs related to nuclear spliceosomal introns and eukaryotic retrotransposons. They self-splice, yielding mature RNA, and integrate into DNA as retroelements. A fully active group II intron forms a ribonucleoprotein complex comprising the intron ribozyme and an intron-encoded protein that performs multiple activities including reverse transcription, in which intron RNA is copied into the DNA target. Here we report cryo-EM structures of an endogenously spliced Lactococcus lactis group IIA intron in its ribonucleoprotein complex form at 3.8-Å resolution and in its protein-depleted form at 4.5-Å resolution, revealing functional coordination of the intron RNA with the protein. Remarkably, the protein structure reveals a close relationship between the reverse transcriptase catalytic domain and telomerase, whereas the active splicing center resembles the spliceosomal Prp8 protein. These extraordinary similarities hint at intricate ancestral relationships and provide new insights into splicing and retromobility.


  • Organizational Affiliation

    Department of Biological Sciences and RNA Institute, University at Albany, Albany, New York, USA.


Macromolecules
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Entity ID: 1
MoleculeChains LengthOrganismImage
GROUP II INTRON704Lactococcus lactis
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: ELECTRON MICROSCOPY
  • Resolution: 4.50 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2016-05-04
    Type: Initial release
  • Version 1.1: 2016-05-11
    Changes: Database references
  • Version 1.2: 2016-06-22
    Changes: Database references
  • Version 1.3: 2024-05-08
    Changes: Data collection, Database references