Purification, crystallization and preliminary crystallographic analysis of avian infectious bronchitis virus nsp3 ADRP domain
- 9 August 2008
- journal article
- research article
- Published by International Union of Crystallography (IUCr) in Acta Crystallographica Section F Structural Biology and Crystallization Communications
- Vol. 64 (9) , 802-804
- https://doi.org/10.1107/s1744309108024391
Abstract
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 P1, with unit-cell parameters a = 41.1, b = 43.2, c = 48.9 Å, = 78.0, = 80.0, = 73.6°. Each asymmetric unit contains two molecules.Keywords
This publication has 6 references indexed in Scilit:
- Coronavirus avian infectious bronchitis virusVeterinary Research, 2007
- The macro domain is an ADP-ribose binding moduleThe EMBO Journal, 2005
- Structure and mechanism of ADP‐ribose‐1″‐monophosphatase (Appr‐1″‐pase), a ubiquitous cellular processing enzymeProtein Science, 2005
- Identification and Characterization of Severe Acute Respiratory Syndrome Coronavirus Replicase ProteinsJournal of Virology, 2004
- Unique and Conserved Features of Genome and Proteome of SARS-coronavirus, an Early Split-off From the Coronavirus Group 2 LineagePublished by Elsevier ,2003
- Processing of X-ray diffraction data collected in oscillation mode.1997