PDBsum entry 5evm

Viral protein

PDB id: 5evm

Contents

Protein chains

(+ 0 more) 456 a.a.

Ligands

NAG-NAG-BMA-MAN-MAN

NAG-NAG ×5

NAG-NAG-MAN ×6

NAG-NAG-MAN-MAN-MAN ×3

NAG-NAG-MAN-MAN ×3

MLI ×6

PDB id:

5evm

Name:

Viral protein

Title:

Crystal structure of nipah virus fusion glycoprotein in the prefusion state

Structure:

Fusion glycoprotein f0. Chain: a, b, c, d, e, f. Synonym: protein f. Engineered: yes. Mutation: yes

Source:

Nipah virus. Organism_taxid: 121791. Expressed in: homo sapiens. Expression_system_taxid: 9606. Expression_system_organ: kidney. Expression_system_cell: epithelia

Resolution:

3.37Å R-factor: 0.214 R-free: 0.220

Authors:

K.Xu,D.B.Nikolov

Key ref:

K.Xu et al. (2015). Crystal Structure of the Pre-fusion Nipah Virus Fusion Glycoprotein Reveals a Novel Hexamer-of-Trimers Assembly. Plos Pathog, 11, e1005322. PubMed id: 26646856 DOI: 10.1371/journal.ppat.1005322

Date:

20-Nov-15 Release date: 16-Dec-15

Protein chains

Q9IH63  (FUS_NIPAV) -  Fusion glycoprotein F0 from Nipah virus

Seq: 546 a.a.

Struc: 456 a.a.*

* PDB and UniProt seqs differ at 2 residue positions (black crosses)

DOI no: 10.1371/journal.ppat.1005322

Plos Pathog 11:e1005322 (2015)

PubMed id: 26646856

Crystal Structure of the Pre-fusion Nipah Virus Fusion Glycoprotein Reveals a Novel Hexamer-of-Trimers Assembly.

K.Xu, Y.P.Chan, B.Bradel-Tretheway, Z.Akyol-Ataman, Y.Zhu, S.Dutta, L.Yan, Y.Feng, L.F.Wang, G.Skiniotis, B.Lee, Z.H.Zhou, C.C.Broder, H.C.Aguilar, D.B.Nikolov.

ABSTRACT

Nipah virus (NiV) is a paramyxovirus that infects host cells through the coordinated efforts of two envelope glycoproteins. The G glycoprotein attaches to cell receptors, triggering the fusion (F) glycoprotein to execute membrane fusion. Here we report the first crystal structure of the pre-fusion form of the NiV-F glycoprotein ectodomain. Interestingly this structure also revealed a hexamer-of-trimers encircling a central axis. Electron tomography of Nipah virus-like particles supported the hexameric pre-fusion model, and biochemical analyses supported the hexamer-of-trimers F assembly in solution. Importantly, structure-assisted site-directed mutagenesis of the interfaces between F trimers highlighted the functional relevance of the hexameric assembly. Shown here, in both cell-cell fusion and virus-cell fusion systems, our results suggested that this hexamer-of-trimers assembly was important during fusion pore formation. We propose that this assembly would stabilize the pre-fusion F conformation prior to cell attachment and facilitate the coordinated transition to a post-fusion conformation of all six F trimers upon triggering of a single trimer. Together, our data reveal a novel and functional pre-fusion architecture of a paramyxoviral fusion glycoprotein.