3WI0
P453H/I471T mutant of PB2 middle domain from influenza virus A/Puerto Rico/8/34(H1N1)
Summary for 3WI0
| Entry DOI | 10.2210/pdb3wi0/pdb |
| Related | 3CW4 3WI1 |
| Descriptor | Polymerase basic protein 2 (2 entities in total) |
| Functional Keywords | influenza a virus, pb2, middle domain, cap binding, viral protein |
| Biological source | Influenza A virus |
| Cellular location | Virion: P03428 |
| Total number of polymer chains | 1 |
| Total formula weight | 19635.78 |
| Authors | Tsurumura, T.,Yoshida, T.,Tsuge, H. (deposition date: 2013-09-04, release date: 2013-12-18, Last modification date: 2023-11-08) |
| Primary citation | Tsurumura, T.,Qiu, H.,Yoshida, T.,Tsumori, Y.,Hatakeyama, D.,Kuzuhara, T.,Tsuge, H. Conformational Polymorphism of m7GTP in Crystal Structure of the PB2 Middle Domain from Human Influenza A Virus Plos One, 8:e82020-e82020, 2013 Cited by PubMed Abstract: Influenza pandemics with human-to-human transmission of the virus are of great public concern. It is now recognized that a number of factors are necessary for human transmission and virulence, including several key mutations within the PB2 subunit of RNA-dependent RNA polymerase. The structure of the middle domain in PB2 has been revealed with or without m(7)GTP, thus the middle domain is considered to be novel target for structure-based drug design. Here we report the crystal structure of the middle domain of H1N1 PB2 with or without m(7)GTP at 1.9 Å and 2.0 Å resolution, respectively, which has two mutations (P453H, I471T) to increase electrostatic potential and solubility. Here we report the m(7)GTP has unique conformation differ from the reported structure. 7-methyl-guanine is fixed in the pocket, but particularly significant change is seen in ribose and triphosphate region: the buried 7-methyl-guanine indeed binds in the pocket forming by H357, F404, E361 and K376 but the triphosphate continues directly to the outer domain. The presented conformation of m(7)GTP may be a clue for the anti-influenza drug-design. PubMed: 24312396DOI: 10.1371/journal.pone.0082020 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.998 Å) |
Structure validation
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