5FVC: Structure of RNA-bound decameric HMPV nucleoprotein

Citation:
Abstract
Non-segmented, (-)RNA viruses cause serious human diseases. Human metapneumovirus (HMPV), an emerging pathogen of this order of viruses (Mononegavirales) is one of the main causes of respiratory tract illness in children. To help elucidate the assembly mechanism of the nucleocapsid (the viral RNA genome packaged by the nucleoprotein N) we present crystallographic structures of HMPV N in its assembled RNA-bound state and in a monomeric state, bound to the polymerase cofactor P. Our structures reveal molecular details of how P inhibits the self-assembly of N and how N transitions between the RNA-free and RNA-bound conformational state. Notably, we observe a role for the C-terminal extension of N in directly preventing premature uptake of RNA by folding into the RNA-binding cleft. Our structures suggest a common mechanism of how the growth of the nucleocapsid is orchestrated, and highlight an interaction site representing an important target for antivirals.
PDB ID: 5FVCDownload
MMDB ID: 136790
PDB Deposition Date: 2016/2/5
Updated in MMDB: 2017/03
Experimental Method:
x-ray diffraction
Resolution: 4.17  Å
Source Organism:
Escherichia coli BL21(DE3)
Similar Structures:
Biological Unit for 5FVC: undecameric; determined by software (PISA)
Molecular Components in 5FVC
Label Count Molecule
Proteins (10 molecules)
10
Hmpv Nucleoprotein
Molecule annotation
Nucleotide(1 molecule)
1
RNA
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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