4PMI

Crystal structure of Rev and Rev-response-element RNA complex

Summary for 4PMI

• Entry DOI: 10.2210/pdb4pmi/pdb
• Descriptor: Rev-Response-Element RNA, Protein Rev, PHOSPHATE ION, ... (4 entities in total)
• Functional Keywords: protein-rna complex, helix-loop-helix, hiv, nuclear export, rna binding protein-rna complex, rna binding protein/rna
• Biological source: Human immunodeficiency virus type 1 group M subtype B (HIV-1); More
• Total number of polymer chains: 3
• Total formula weight: 29795.51

Authors

Jayaraman, B.,Crosby, D.C.,Homer, C.,Ribeiro, I.,Mavor, D.,Frankel, A.D. (deposition date: 2014-05-21, release date: 2014-12-24, Last modification date: 2023-09-27)

Primary citation

Jayaraman, B.,Crosby, D.C.,Homer, C.,Ribeiro, I.,Mavor, D.,Frankel, A.D.
RNA-directed remodeling of the HIV-1 protein Rev orchestrates assembly of the Rev-Rev response element complex.
Elife, 4:e04120-e04120, 2014

PubMed Abstract: The HIV-1 protein Rev controls a critical step in viral replication by mediating the nuclear export of unspliced and singly-spliced viral mRNAs. Multiple Rev subunits assemble on the Rev Response Element (RRE), a structured region present in these RNAs, and direct their export through the Crm1 pathway. Rev-RRE assembly occurs via several Rev oligomerization and RNA-binding steps, but how these steps are coordinated to form an export-competent complex is unclear. Here, we report the first crystal structure of a Rev dimer-RRE complex, revealing a dramatic rearrangement of the Rev-dimer upon RRE binding through re-packing of its hydrophobic protein-protein interface. Rev-RNA recognition relies on sequence-specific contacts at the well-characterized IIB site and local RNA architecture at the second site. The structure supports a model in which the RRE utilizes the inherent plasticity of Rev subunit interfaces to guide the formation of a functional complex.

PubMed: 25486594
DOI: 10.7554/eLife.04120

Experimental method

X-RAY DIFFRACTION (3.2 Å)