PDBsum entry 5fvc

Viral protein

PDB id: 5fvc

Contents

Protein chains

346 a.a.

(+ 2 more) 367 a.a.

DNA/RNA

PDB id:

5fvc

Name:

Viral protein

Title:

Structure of RNA-bound decameric hmpv nucleoprotein

Structure:

Hmpv nucleoprotein. Chain: a, b, c, d, e, f, g, h, i, j. Engineered: yes. RNA. Chain: k. Other_details: e. Coli RNA

Source:

Human metapneumovirus. Organism_taxid: 162145. Strain: nl1-00. Variant: a1. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Expression_system_variant: rosetta2. Escherichia coli. Organism_taxid: 469008.

Resolution:

4.17Å R-factor: 0.193 R-free: 0.230

Authors:

M.Renner,M.Bertinelli,C.Leyrat,G.C.Paesen,L.F.Saraiva De Oliveira, J.T.Huiskonen,J.M.Grimes

Key ref:

M.Renner et al. (2016). Nucleocapsid assembly in pneumoviruses is regulated by conformational switching of the N protein. Elife, 5, e12627. PubMed id: 26880565 DOI: 10.7554/eLife.12627

Date:

05-Feb-16 Release date: 24-Feb-16

Protein chains

Q91F57  (Q91F57_9MONO) -  Nucleoprotein from Human metapneumovirus

Seq: 394 a.a.

Struc: 346 a.a.

Protein chains

Q91F57  (Q91F57_9MONO) -  Nucleoprotein from Human metapneumovirus

Seq: 394 a.a.

Struc: 367 a.a.

DNA/RNA chain

C-C-C-C-C-C-C-C-C-C-C-C-C-C-C-C-C-C-C-C-C-C-C-C-C-C-C-C-C-C-C-C-C-C-C-C-C-C-C- 70 bases

Enzyme reactions

• Enzyme class: Chains A, B, C, D, E, F, G, H, I, J: E.C.?

DOI no: 10.7554/eLife.12627

Elife 5:e12627 (2016)

PubMed id: 26880565

Nucleocapsid assembly in pneumoviruses is regulated by conformational switching of the N protein.

M.Renner, M.Bertinelli, C.Leyrat, G.C.Paesen, L.F.Saraiva de Oliveira, J.T.Huiskonen, J.M.Grimes.

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.