Open AccessPurification, crystallization and preliminary crystallographic analysis of avian infectious bronchitis virus nsp3 ADRP domain
Author(s) -
Wei Lei,
Chen Cheng,
Zhao Qi,
Li Chun,
Cong Le,
Xu Xiaoling,
Ma Yanlin,
Liao Ming,
Xu Yuanyuan,
Rao Zihe
Publication year - 2008
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309108024391
Subject(s) - biology , escherichia coli , rna splicing , transcription (linguistics) , infectious bronchitis virus , ribose , rna , gene , microbiology and biotechnology , biochemistry , enzyme , linguistics , philosophy
Avian infectious bronchitis virus (IBV) encodes 15 nonstructural proteins (nsps) which play crucial roles in RNA transcription and genome replication. One of them, nsp3, contains an ADRP (adenosine diphosphate‐ribose‐1′‐phosphatase) domain which was revealed in recent studies to have ADP‐ribose‐1′‐monophosphatase (Appr‐1′‐pase) activity. Appr‐1′‐pase catalyzes the conversion of ADP‐ribose‐1′‐monophosphate (Appr‐1′‐p) to ADP‐ribose in the tRNA‐splicing pathway. The gene segment encoding the IBV nsp3 ADRP domain has been cloned and expressed in Escherichia coli . The protein has been crystallized and the crystals diffracted to 1.8 Å resolution. They belonged to space group P 1, with unit‐cell parameters a = 41.1, b = 43.2, c = 48.9 Å, α = 78.0, β = 80.0, γ = 73.6°. Each asymmetric unit contains two molecules.