| Title | Crystallization and X-ray crystallographic analysis of the cap-binding domain of influenza A virus H1N1 polymerase subunit PB2 |
| Authors | Liu, Yong Meng, Geng Luo, Ming Zheng, Xiaofeng |
| Affiliation | Peking Univ, Sch Life Sci, State Key Lab Prot & Plant Gene Res, Beijing 100871, Peoples R China. Peking Univ, Sch Life Sci, Dept Biochem & Mol Biol, Beijing 100871, Peoples R China. Univ Alabama Birmingham, Dept Microbiol, Birmingham, AL 35294 USA. |
| Keywords | PB2 cap-binding protein PROTEIN EIF4E ENDONUCLEASE SITE |
| Issue Date | 2013 |
| Publisher | acta crystallographica section f structural biology and crystallization communications |
| Citation | ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS.2013,69,280-283. |
| Abstract | PB2 is one of the subunits of the influenza virus heterotrimeric polymerase. By its cap-binding domain (PB2cap), PB2 captures the 5 cap of the host pre-mRNA to generate a capped 5 oligonucleotide primer for virus transcription. The crystal structure of influenza A virus H3N2 PB2cap with bound cap analogue m7GTP has been reported previously. To show the substrate-free structural details of PB2cap and clarify whether obvious conformational changes exist between the substrate-free and substrate-bound cap-binding domain, we have successfully obtained the crystal of substrate-free H1N1 PB2cap. The crystal of H1N1 PB2cap diffracted to a high resolution of 1.32 angstrom. The crystal symmetry belongs to space group P1 with unit-cell parameters a = 29.49, b = 37.04, c = 38.33 angstrom, = 71.10, = 69.84, = 75.85 degrees. There is one molecule in the asymmetric unit. |
| URI | http://hdl.handle.net/20.500.11897/190364 |
| ISSN | 1744-3091 |
| DOI | 10.1107/S1744309113002388 |
| Indexed | SCI(E) PubMed |
| Appears in Collections: | 生命科学学院 |
