PDBsum entry 4ypi

RNA binding protein

PDB id: 4ypi

Contents

Protein chains

348 a.a.

28 a.a.

PDB id:

4ypi

Name:

RNA binding protein

Title:

Structure of ebola virus nucleoprotein n-terminal fragment bound to a peptide derived from ebola vp35

Structure:

Nucleoprotein. Chain: c, a, b, d. Synonym: nucleocapsid protein,protein n. Engineered: yes. Polymerase cofactor vp35. Chain: g, e, f, h. Engineered: yes

Source:

Zaire ebolavirus (strain mayinga-76). Zebov. Organism_taxid: 128952. Strain: mayinga-76. Gene: np. Expressed in: escherichia coli. Expression_system_taxid: 469008. Synthetic: yes. Organism_taxid: 128952

Resolution:

3.71Å R-factor: 0.255 R-free: 0.285

Authors:

D.W.Leung,D.M.Borek,J.M.Binning,Z.Otwinowski,G.K.Amarasinghe,Center For Structural Genomics Of Infectious Diseases (Csgid)

Key ref:

D.W.Leung et al. (2015). An Intrinsically Disordered Peptide from Ebola Virus VP35 Controls Viral RNA Synthesis by Modulating Nucleoprotein-RNA Interactions. Cell Rep, 11, 376-389. PubMed id: 25865894 DOI: 10.1016/j.celrep.2015.03.034

Date:

13-Mar-15 Release date: 08-Apr-15

Protein chains

P18272  (NCAP_EBOZM) -  Nucleoprotein from Zaire ebolavirus (strain Mayinga-76)

Seq: 739 a.a.

Struc: 348 a.a.

Protein chains

Q05127  (VP35_EBOZM) -  Polymerase cofactor VP35 from Zaire ebolavirus (strain Mayinga-76)

Seq: 340 a.a.

Struc: 28 a.a.

DOI no: 10.1016/j.celrep.2015.03.034

Cell Rep 11:376-389 (2015)

PubMed id: 25865894

An Intrinsically Disordered Peptide from Ebola Virus VP35 Controls Viral RNA Synthesis by Modulating Nucleoprotein-RNA Interactions.

D.W.Leung, D.Borek, P.Luthra, J.M.Binning, M.Anantpadma, G.Liu, I.B.Harvey, Z.Su, A.Endlich-Frazier, J.Pan, R.S.Shabman, W.Chiu, R.A.Davey, Z.Otwinowski, C.F.Basler, G.K.Amarasinghe.

ABSTRACT

During viral RNA synthesis, Ebola virus (EBOV) nucleoprotein (NP) alternates between an RNA-template-bound form and a template-free form to provide the viral polymerase access to the RNA template. In addition, newly synthesized NP must be prevented from indiscriminately binding to noncognate RNAs. Here, we investigate the molecular bases for these critical processes. We identify an intrinsically disordered peptide derived from EBOV VP35 (NPBP, residues 20-48) that binds NP with high affinity and specificity, inhibits NP oligomerization, and releases RNA from NP-RNA complexes in vitro. The structure of the NPBP/ΔNPNTD complex, solved to 3.7 Å resolution, reveals how NPBP peptide occludes a large surface area that is important for NP-NP and NP-RNA interactions and for viral RNA synthesis. Together, our results identify a highly conserved viral interface that is important for EBOV replication and can be targeted for therapeutic development.