4GEZ

Structure of a neuraminidase-like protein from A/bat/Guatemala/164/2009

Summary for 4GEZ

• Entry DOI: 10.2210/pdb4gez/pdb
• Related: 4GDI 4GDJ
• Descriptor: Neuraminidase, alpha-L-fucopyranose-(1-6)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[beta-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose, ... (7 entities in total)
• Functional Keywords: influenza virus, coat protein, neuraminidase-like protein, viral protein
• Biological source: Influenza A virus
• Total number of polymer chains: 12
• Total formula weight: 509218.59

Authors

Yang, H.,Carney, P.J.,Donis, R.O.,Stevens, J. (deposition date: 2012-08-02, release date: 2012-09-26, Last modification date: 2024-11-06)

Primary citation

Zhu, X.,Yang, H.,Guo, Z.,Yu, W.,Carney, P.J.,Li, Y.,Chen, L.M.,Paulson, J.C.,Donis, R.O.,Tong, S.,Stevens, J.,Wilson, I.A.
Crystal structures of two subtype N10 neuraminidase-like proteins from bat influenza A viruses reveal a diverged putative active site.
Proc.Natl.Acad.Sci.USA, 109:18903-18908, 2012

PubMed Abstract: Recently, we reported a unique influenza A virus subtype H17N10 from little yellow-shouldered bats. Its neuraminidase (NA) gene encodes a protein that appears to be highly divergent from all known influenza NAs and was assigned as a new subtype N10. To provide structural and functional insights on the bat H17N10 virus, X-ray structures were determined for N10 NA proteins from influenza A viruses A/little yellow-shouldered bat/Guatemala/164/2009 (GU09-164) in two crystal forms at 1.95 Å and 2.5 Å resolution and A/little yellow-shouldered bat/Guatemala/060/2010 (GU10-060) at 2.0 Å. The overall N10 structures are similar to each other and to other known influenza NA structures, with a single highly conserved calcium binding site in each monomer. However, the region corresponding to the highly conserved active site of influenza A N1-N9 NA subtypes and influenza B NA differs substantially. In particular, most of the amino acid residues required for NA activity are substituted, and the putative active site is much wider because of displacement of the 150-loop and 430-loop. These structural features and the fact that the recombinant N10 protein exhibits no, or extremely low, NA activity suggest that it may have a different function than the NA proteins of other influenza viruses. Accordingly, we propose that the N10 protein be termed an NA-like protein until its function is elucidated.

PubMed: 23012478
DOI: 10.1073/pnas.1212579109

Experimental method

X-RAY DIFFRACTION (2.5 Å)