7NN9 | Hydrolase (O-Glycosyl) | date | Mar 15, 1995 ![]() ![]() |
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title | Native Influenza Virus Neuraminidase Subtype N9 (Tern) | ||||||||||||||
authors | J.N.Varghese, P.M.Colman | ||||||||||||||
compound | source | ||||||||||||||
Molecule: Neuraminidase N9 Chain: A Synonym: Sialidase Ec: 3.2.1.18 |
Organism_scientific: Influenza A Virus (Aternaustraliag70c1975(H11n9)); Organism_taxid: 384509 Strain: Aternaustraliag70c75 | ||||||||||||||
symmetry | Space Group: I 4 3 2 |
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crystal cell |
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method | X-Ray Diffraction | resolution | 2 Å | ||||||||||||
ligand | CA, MAN, NAG | enzyme | Exo-alpha-sialidase;. Neuraminidase;. Sialidase;. Alpha-neuraminidase;. Acetylneuraminidase. Hydrolase E.C.3.2.1.18 BRENDA | ||||||||||||
note | 7NN9 supersedes 2NN9 | ||||||||||||||
related structures | by homologous chain: 1BJI, 2QWE | ||||||||||||||
domain | The transmembrane domain also plays a role in lipid raft association (by similarity). Intact n-terminus is essential for virion morphogenesis. Possess two apical sorting signals, one in the ectodomain, which is likely to be a glycan, and the other in the transmembrane domain. | ||||||||||||||
similarity | Belongs to the glycosyl hydrolase 34 family.[Neur] | ||||||||||||||
subunit | Homotetramer (by similarity). | ||||||||||||||
catalytic activ. | 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. | ||||||||||||||
post-translat. modifications | N-glycosylated (by similarity). | ||||||||||||||
subcellular loc. | Preferentially accumulates at the apical plasma membrane in infected polarized epithelial cells, which is the virus assembly site. Uses lipid rafts for cell surface transport and apical sorting. Type ii membrane protein. In the virion, forms a mushroom-shaped spike on the surface of the membrane (by similarity). | ||||||||||||||
enzyme regulation | These drugs interfere with the release of progeny virus from infected cells and are effective against all influenza strains. Inhibited by the neuraminidase inhibitors zanamivir (relenza) and oseltamivir (tamiflu). Resistance to neuraminidase inhibitors is quite rare. | ||||||||||||||
Gene | NA | ||||||||||||||
function | Catalyzes the removal of terminal sialic acid residues from viral and cellular glycoconjugates. May facilitate viral invasion of the upper airways by cleaving the sialic acid moities on the mucin of the airway epithelial cells. Described as a receptor-destroying enzyme because it cleaves a terminal sialic acid from the cellular receptors. Otherwise, infection would be limited to one round of replication. Cleaves off the terminal sialic acids on the glycosylated ha during virus budding to facilitate virus release. Likely to plays a role in the budding process through its association with lipid rafts during intracellular transport. Additionally helps virus spread through the circulation by further removing sialic acids from the cell surface. These cleavages prevent self-aggregation and ensure the efficient spread of the progeny virus from cell to cell. Plays a role in the determination of host range restriction on replication and virulence. Sialidase activity in late endosome/lysosome traffic seems to enhance virus replication. May additionally display a raft-association independent effect on budding. | ||||||||||||||
Gene Ontology | |||||||||||||||
Primary reference | Three-dimensional structure of the complex of 4-guanidino-Neu5Ac2en and influenza virus neuraminidase., Varghese JN, Epa VC, Colman PM, Protein Sci 1995 Jun;4(6):1081-7. PMID:7549872 |
Data retrieval |
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View 7NN9 in 3D |
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Visual 3D analysis of 7NN9 |
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Structure-derived information |
- Domain d7nn9__, region [Jmol] [rasmolscript] [script source] |
Sequence-derived information |
Other resources with information on 7NN9 |
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