4nfz | pdb_00004nfz

Crystal structure of polymerase subunit PA N-terminal endonuclease domain from bat-derived influenza virus H17N10

spinqualitylabelsall models 4nfz, resolution 2.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4nfz is a 3 chain structure with sequence from Influenza A virus (A/little yellow-shouldered bat/Guatemala/060/2010(H17N10)). Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.7Å Ligands: MN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function H6QM92_9INFA Publication Abstract from PubMed Influenza imposes a great burden on society, not only in its seasonal appearance that affects both humans and domesticated animals, but also through the constant threat of potential pandemics. Migratory birds are considered to be the reservoir hosts for influenza viruses, but other animals must also be considered. The recently identified influenza-like virus genome, H17N10, in bats, was shown to be markedly different from other known influenza viruses, as both its surface glycoproteins hemagglutinin (HA) and neuraminidase (NA) do not have canonical functions. However no studies on other individual proteins from this particular virus have been reported until now. Here, we describe the structure of the N-terminal domain of PA from H17N10 influenza-like virus at 2.7 A resolution and show that it has a similar fold as homologous PA domains present in more familiar influenza A strains. Moreover, we demonstrate that it possesses endonuclease activity and that the histidine residue in the active site is essential for this activity. Although this particular influenza subtype is probably not infectious for humans (even its virus state has not been confirmed in bat as only the genome has been sequenced), reassortment of canonical influenza viruses with certain segments from H17N10 cannot be ruled out at this stage. Therefore further studies are urgently called for the sake of influenza prevention and control. The N-terminal domain of PA from bat-derived influenza-like virus H17N10 has endonuclease activity.,Tefsen B, Lu G, Zhu Y, Haywood J, Zhao L, Deng T, Qi J, Gao GF J Virol. 2013 Nov 27. PMID:24284327 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also RNA polymerase 3D structures

Proteopedia Page Contributors and Editors (what is this?)

OCA