Open AccessCrystallization and X‐ray crystallographic analysis of the cap‐binding domain of influenza A virus H1N1 polymerase subunit PB2
Author(s) -
Liu Yong,
Meng Geng,
Luo Ming,
Zheng Xiaofeng
Publication year - 2013
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309113002388
Subject(s) - heterotrimeric g protein , polymerase , crystallography , crystallization , protein subunit , virus , influenza a virus , chemistry , biology , biophysics , virology , dna , biochemistry , gene , receptor , g protein , organic chemistry
PB2 is one of the subunits of the influenza virus heterotrimeric polymerase. By its cap‐binding domain (PB2 cap ), 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 PB2 cap with bound cap analogue m 7 GTP has been reported previously. To show the substrate‐free structural details of PB2 cap 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 PB2 cap . The crystal of H1N1 PB2 cap diffracted to a high resolution of 1.32 Å. The crystal symmetry belongs to space group P 1 with unit‐cell parameters a = 29.49, b = 37.04, c = 38.33 Å, α = 71.10, β = 69.84, γ = 75.85°. There is one molecule in the asymmetric unit.