PDBsum entry 5e65

Hydrolase

PDB id: 5e65

Contents

Protein chains

424 a.a.

149 a.a.

Ligands

NAG-NAG-BMA-MAN-MAN-MAN ×3

NAG-NAG ×5

GAL-5N6 ×2

NAG ×2

Waters ×675

PDB id:

5e65

Name:

Hydrolase

Title:

The complex structure of hemagglutinin-esterase-fusion mutant protein from the influenza d virus with receptor analog 9-o-ac-3'sln (tr322)

Structure:

Hemagglutinin-esterase. Chain: a, c. Fragment: unp residues 19-445. Engineered: yes. Mutation: yes. Hemagglutinin-esterase. Chain: b, d. Fragment: unp residues 456-621. Engineered: yes

Source:

Influenza d virus (d/swine/oklahoma/1334/2011). Organism_taxid: 1173138. Strain: d/swine/oklahoma/1334/2011. Gene: hef. Expressed in: trichoplusia ni. Expression_system_taxid: 7111. Expression_system_cell_line: hi5. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108

Resolution:

2.20Å R-factor: 0.206 R-free: 0.243

Authors:

H.Song,J.Qi,Y.Shi,G.F.Gao

Key ref:

H.Song et al. (2016). An Open Receptor-Binding Cavity of Hemagglutinin-Esterase-Fusion Glycoprotein from Newly-Identified Influenza D Virus: Basis for Its Broad Cell Tropism. PLoS Pathog, 12, e1005411. PubMed id: 26816272

Date:

09-Oct-15 Release date: 23-Mar-16

Protein chains

K9LG83  (K9LG83_9ORTO) -  Hemagglutinin-esterase-fusion glycoprotein from Influenza D virus

Seq: 664 a.a.

Struc: 424 a.a.*

Protein chains

K9LG83  (K9LG83_9ORTO) -  Hemagglutinin-esterase-fusion glycoprotein from Influenza D virus

Seq: 664 a.a.

Struc: 149 a.a.

* PDB and UniProt seqs differ at 3 residue positions (black crosses)

Enzyme reactions

• Enzyme class: Chains A, B, C, D: E.C.3.1.1.53 - sialate O-acetylesterase.
• Reaction:
  1. N-acetyl-9-O-acetylneuraminate + H2O = N-acetylneuraminate + acetate + H⁺
  2. N-acetyl-4-O-acetylneuraminate + H2O = N-acetylneuraminate + acetate + H⁺

N-acetyl-9-O-acetylneuraminate + H2O (Bound ligand (Het Group name = 5N6) matches with 95.83% similarity) = N-acetylneuraminate + acetate + H(+)

N-acetyl-4-O-acetylneuraminate + H2O = N-acetylneuraminate + acetate + H(+) (Bound ligand (Het Group name = 5N6) matches with 83.33% similarity)

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

PLoS Pathog 12:e1005411 (2016)

PubMed id: 26816272

An Open Receptor-Binding Cavity of Hemagglutinin-Esterase-Fusion Glycoprotein from Newly-Identified Influenza D Virus: Basis for Its Broad Cell Tropism.

H.Song, J.Qi, Z.Khedri, S.Diaz, H.Yu, X.Chen, A.Varki, Y.Shi, G.F.Gao.

ABSTRACT

Influenza viruses cause seasonal flu each year and pandemics or epidemic sporadically, posing a major threat to public health. Recently, a new influenza D virus (IDV) was isolated from pigs and cattle. Here, we reveal that the IDV utilizes 9-O-acetylated sialic acids as its receptor for virus entry. Then, we determined the crystal structures of hemagglutinin-esterase-fusion glycoprotein (HEF) of IDV both in its free form and in complex with the receptor and enzymatic substrate analogs. The IDV HEF shows an extremely similar structural fold as the human-infecting influenza C virus (ICV) HEF. However, IDV HEF has an open receptor-binding cavity to accommodate diverse extended glycan moieties. This structural difference provides an explanation for the phenomenon that the IDV has a broad cell tropism. As IDV HEF is structurally and functionally similar to ICV HEF, our findings highlight the potential threat of the virus to public health.