4QN4

Crystal structure of Neuraminidase N6

Summary for 4QN4

• Entry DOI: 10.2210/pdb4qn4/pdb
• Related: 4QN3 4QN5 4QN6 4QN7
• Descriptor: Neuraminidase, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (7 entities in total)
• Functional Keywords: 6-bladed beta-propeller, hydrolase, calcium binding, glycosylation
• Biological source: Influenza A virus (A/chicken/Nanchang/7-010/2000(H3N6))
• Cellular location: Virion membrane: Q2FCL6
• Total number of polymer chains: 2
• Total formula weight: 90681.81

Authors

Sun, X.,Li, Q.,Wu, Y.,Liu, Y.,Qi, J.,Vavricka, C.J.,Gao, G.F. (deposition date: 2014-06-17, release date: 2014-07-30, Last modification date: 2024-10-30)

Primary citation

Sun, X.,Li, Q.,Wu, Y.,Wang, M.,Liu, Y.,Qi, J.,Vavricka, C.J.,Gao, G.F.
Structure of influenza virus N7: the last piece of the neuraminidase "jigsaw" puzzle.
J.Virol., 88:9197-9207, 2014

PubMed Abstract: There are nine subtypes of influenza A virus neuraminidase (NA), N1 to N9. In addition, influenza B virus also contains NA, and there are two influenza virus NA-like molecules, N10 and N11, which were recently identified from bats. Crystal structures for all of these proteins have been solved, with the exception of N7, and there is no published report of N6, although a structure has been deposited in the Protein Data Bank. Here, we present the N7 and N6 structures at 2.1 Å and 1.8 Å, respectively. Structural comparison of all NA subtypes shows that both N7 and N6 highly resemble typical group 2 NA structures with some special characteristics, including an additional cavity adjacent to their active sites formed by novel 340-loop conformations. Comparative analysis also revealed new structural insights into the N-glycosylation, calcium binding, and second sialic acid binding site of influenza virus NA. This comprehensive study is critical for understanding the complexity of the most successful influenza drug target and for the structure-based design of novel influenza inhibitors.

PubMed: 24899180
DOI: 10.1128/JVI.00805-14

Experimental method

X-RAY DIFFRACTION (1.8 Å)