4WEG
influenza virus neuraminidase N9 in complex 2,3-difluorosialic acid
Summary for 4WEG
| Entry DOI | 10.2210/pdb4weg/pdb |
| Related | 1NNC 4WEF |
| Descriptor | Neuraminidase, alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-3)-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, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (9 entities in total) |
| Functional Keywords | influenza virus neuraminidase, n9, complex, 2, 3-difluorosialic acid, second binding site, hydrolase |
| Biological source | Influenza A virus (A/tern/Australia/G70C/1975(H11N9)) |
| Cellular location | Virion membrane : P03472 |
| Total number of polymer chains | 1 |
| Total formula weight | 46772.46 |
| Authors | Streltsov, V.A.,Pilling, P.,Barrett, S.,McKimm-Breschkin, J. (deposition date: 2014-09-10, release date: 2015-09-16, Last modification date: 2024-11-13) |
| Primary citation | Streltsov, V.A.,Pilling, P.,Barrett, S.,McKimm-Breschkin, J.L. Catalytic mechanism and novel receptor binding sites of human parainfluenza virus type 3 hemagglutinin-neuraminidase (hPIV3 HN) Antiviral Res., 123:216-223, 2015 Cited by PubMed Abstract: The human parainfluenza virus type 3 (hPIV3) hemagglutinin-neuraminidase (HN) has opposing functions of binding sialic acid receptors and cleaving them, facilitating virus release. The crystal structure of hPIV3 HN complexed with the substrate analogue difluorosialic acid (DFSA) revealed that catalysis by HN involves the formation of a covalently linked sialosyl-enzyme intermediate which was trapped along with a transition-state analogue resembling an oxocarbenium ion. This mechanism of enzyme catalysis was also confirmed in the crystal structure of the influenza N9 neuraminidase complexed with DFSA. Additionally, novel secondary receptor binding sites were identified in the hPIV3 HN-DFSA complex including one near the catalytic cavity which upon binding DFSA imposes subtle changes and may help the HN balance the opposing functions. Multiple receptor binding sites may increase avidity to facilitate cell binding and fusion promotion. The secondary receptor binding sites in the paramyxoviruses are so far unique to each virus type. PubMed: 26364554DOI: 10.1016/j.antiviral.2015.08.014 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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