Faculty Opinions recommendation of Crystal structure of the rabies virus nucleoprotein-RNA complex.

ABSTRACT The crystal structure of the dimerization domain of rabies virus phosphoprotein was determined. The monomer consists of two α-helices that make a helical hairpin held together mainly by hydrophobic interactions. The monomer has a hydrophilic and a hydrophobic face, and in the dimer two monomers pack together through their hydrophobic surfaces. This structure is very different from the dimerization domain of the vesicular stomatitis virus phosphoprotein and also from the tetramerization domain of the Sendai virus phosphoprotein, suggesting that oligomerization is conserved but not structure.

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A crystal structure of a collaborative RNA regulatory complex reveals mechanisms to refine target specificity

eLife ◽

10.7554/elife.48968 ◽

2019 ◽

Vol 8 ◽

Cited By ~ 6

Author(s):

Chen Qiu ◽

Vandita D Bhat ◽

Sanjana Rajeev ◽

Chi Zhang ◽

Alexa E Lasley ◽

...

Keyword(s):

Crystal Structure ◽

In Vitro Selection ◽

Rna Binding ◽

Sequence Specificity ◽

Binding Assays ◽

Regulatory Complex ◽

Rna Motif ◽

Rna Complex ◽

Motif Recognition

In the Caenorhabditis elegans germline, fem-3 Binding Factor (FBF) partners with LST-1 to maintain stem cells. A crystal structure of an FBF-2/LST-1/RNA complex revealed that FBF-2 recognizes a short RNA motif different from the characteristic 9-nt FBF binding element, and compact motif recognition coincided with curvature changes in the FBF-2 scaffold. Previously, we engineered FBF-2 to favor recognition of shorter RNA motifs without curvature change (Bhat et al., 2019). In vitro selection of RNAs bound by FBF-2 suggested sequence specificity in the central region of the compact element. This bias, reflected in the crystal structure, was validated in RNA-binding assays. FBF-2 has the intrinsic ability to bind to this shorter motif. LST-1 weakens FBF-2 binding affinity for short and long motifs, which may increase target selectivity. Our findings highlight the role of FBF scaffold flexibility in RNA recognition and suggest a new mechanism by which protein partners refine target site selection.

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Crystal Structure of a Nucleocapsid-Like Nucleoprotein-RNA Complex of Respiratory Syncytial Virus

Science ◽

10.1126/science.1177634 ◽

2009 ◽

Vol 326 (5957) ◽

pp. 1279-1283 ◽

Cited By ~ 204

Author(s):

Rajiv G. Tawar ◽

Stéphane Duquerroy ◽

Clemens Vonrhein ◽

Paloma F. Varela ◽

Laurence Damier-Piolle ◽

...

Keyword(s):

Crystal Structure ◽

Respiratory Syncytial Virus ◽

Rna Virus ◽

Three Dimensional ◽

Detailed Model ◽

Syncytial Virus ◽

Key Sites ◽

Microscopy Data ◽

Nucleoprotein N ◽

Rna Complex

The respiratory syncytial virus (RSV) is an important human pathogen, yet neither a vaccine nor effective therapies are available to treat infection. To help elucidate the replication mechanism of this RNA virus, we determined the three-dimensional (3D) crystal structure at 3.3 Å resolution of a decameric, annular ribonucleoprotein complex of the RSV nucleoprotein (N) bound to RNA. This complex mimics one turn of the viral helical nucleocapsid complex, which serves as template for viral RNA synthesis. The RNA wraps around the protein ring, with seven nucleotides contacting each N subunit, alternating rows of four and three stacked bases that are exposed and buried within a protein groove, respectively. Combined with electron microscopy data, this structure provides a detailed model for the RSV nucleocapsid, in which the bases are accessible for readout by the viral polymerase. Furthermore, the nucleoprotein structure highlights possible key sites for drug targeting.

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