PDBsum entry 1v2i

Hydrolase

PDB id: 1v2i

Contents

Protein chains

431 a.a. *

Ligands

NAG-NAG-BMA-MAN-MAN

NAG-NAG ×2

NAG ×3

PO4 ×2

Metals

_CA ×2

Waters ×372

* Residue conservation analysis

PDB id:

1v2i

Name:

Hydrolase

Title:

Structure of the hemagglutinin-neuraminidase from human parainfluenza virus type iii

Structure:

Hemagglutinin-neuraminidase glycoprotein. Chain: a, b. Fragment: residues 142-572. Synonym: hemagglutinin-neuraminidase, hn. Engineered: yes

Source:

Human parainfluenza virus 3. Organism_taxid: 11216. Expressed in: trichoplusia ni. Expression_system_taxid: 7111. Expression_system_cell_line: high five.

Biol. unit:

Dimer (from PQS)

Resolution:

2.20Å R-factor: 0.185 R-free: 0.259

Authors:

M.C.Lawrence,N.A.Borg,V.A.Streltsov,P.A.Pilling,V.C.Epa,J.N.Varghese, J.L.Mckimm-Breschkin,P.M.Colman

Key ref:

M.C.Lawrence et al. (2004). Structure of the haemagglutinin-neuraminidase from human parainfluenza virus type III. J Mol Biol, 335, 1343-1357. PubMed id: 14729348 DOI: 10.1016/j.jmb.2003.11.032

Date:

16-Oct-03 Release date: 03-Feb-04

Protein chains

Q6WJ03  (Q6WJ03_9MONO) -  Hemagglutinin-neuraminidase glycoprotein from Human respirovirus 3

Seq: 572 a.a.

Struc: 431 a.a.

Enzyme reactions

• Enzyme class: E.C.3.2.1.18 - exo-alpha-sialidase.
• Reaction: Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)-glycosidic linkages of terminal sialic residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates.

DOI no: 10.1016/j.jmb.2003.11.032

J Mol Biol 335:1343-1357 (2004)

PubMed id: 14729348

Structure of the haemagglutinin-neuraminidase from human parainfluenza virus type III.

M.C.Lawrence, N.A.Borg, V.A.Streltsov, P.A.Pilling, V.C.Epa, J.N.Varghese, J.L.McKimm-Breschkin, P.M.Colman.

ABSTRACT

The three-dimensional structure of the haemagglutinin-neuraminidase (HN) from a human parainfluenza virus is described at ca 2.0 A resolution, both in native form and in complex with three substrate analogues. In support of earlier work on the structure of the homologous protein from the avian pathogen Newcastle disease virus (NDV), we observe a dimer of beta-propellers and find no evidence for spatially separated sites performing the receptor-binding and neuraminidase functions of the protein. As with the NDV HN, the active site of the HN of parainfluenza viruses is structurally flexible, suggesting that it may be able to switch between a receptor-binding state and a catalytic state. However, in contrast to the NDV structures, we observe no ligand-induced structural changes that extend beyond the active site and modify the dimer interface.

Selected figure(s)

Figure 3.
Figure 3. Stereo image of the unliganded PIV3 HN active site in the hexagonal (green) and orthorhombic (yellow) crystal forms. Only the "up" conformer of the side-chain of Y530 is shown for the hexagonal crystal form. The two active-site water molecules described in the text, w1 and w2, are shown, colored red for in the hexagonal crystal form and black for in the orthorhombic crystal form. Potential hydrogen bonds are shown as black dotted lines. The Figure was produced using MOLSCRIPT[55.] and Raster3D. [56.]

Figure 4.
Figure 4. Stereo images of the active site of PIV3 HN complexed with (a) b-sialic acid, (b) Neu5Ac2en and (c) zanamivir. Two active-site water molecules are shown (w1 and w2, see the text). Potential hydrogen bonds are shown as black dotted lines. The Figure was produced using MOLSCRIPT[55.] and Raster3D. [56.]

The above figures are reprinted by permission from Elsevier: J Mol Biol (2004, 335, 1343-1357) copyright 2004.

Figures were selected by an automated process.