| Home > Publications database > Structure of the X (ADRP) domain of nsp3 from feline coronavirus |
| Journal Article | PHPPUBDB-12653 |
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2009
Munksgaard
Copenhagen
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Please use a persistent id in citations: doi:10.1107/S0907444909040074
Abstract: The structure of the X (or ADRP) domain of a pathogenic variant of feline coronavirus (FCoV) has been determined in tetragonal and cubic crystal forms to 3.1 and 2.2 A resolution, respectively. In the tetragonal crystal form, glycerol-3-phosphate was observed in the ADP-ribose-binding site. Both crystal forms contained large solvent channels and had a solvent content of higher than 70%. Only very weak binding of this domain to ADP-ribose was detected in vitro. However, the structure with ADP-ribose bound was determined in the cubic crystal form at 3.9 A resolution. The structure of the FCoV X domain had the expected macro-domain fold and is the first structure of this domain from a coronavirus belonging to subgroup 1a.
Keyword(s): Adenosine Diphosphate Ribose: chemistry (MeSH) ; Adenosine Diphosphate Ribose: metabolism (MeSH) ; Amino Acid Sequence (MeSH) ; Binding Sites (MeSH) ; Coronavirus, Feline: enzymology (MeSH) ; Crystallography, X-Ray (MeSH) ; Glycerophosphates: chemistry (MeSH) ; Glycerophosphates: metabolism (MeSH) ; Molecular Sequence Data (MeSH) ; Protein Binding (MeSH) ; Protein Interaction Domains and Motifs (MeSH) ; RNA Replicase: chemistry (MeSH) ; Sequence Alignment (MeSH) ; Sequence Homology, Amino Acid (MeSH) ; Viral Nonstructural Proteins: chemistry (MeSH) ; Glycerophosphates ; Viral Nonstructural Proteins ; Adenosine Diphosphate Ribose ; alpha-glycerophosphoric acid ; RNA Replicase
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