2gth
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crystal structure of the wildtype MHV coronavirus non-structural protein nsp15
OverviewOverview
The unique coronavirus transcription/replication machinery comprised of, multiple virus-encoded nonstructural proteins (nsp) plays a vital role, during initial and intermediate phases of the viral life cycle. The, crystal structure of mouse hepatitis virus strain A59 (MHV-A59) nsp15 is, reported at 2.15-A resolution. nsp15 is an XendoU endoribonuclease and is, the first one from this family to have its structure unveiled. The MHV-A59, nsp15 monomer structure has a novel protein fold. Two nsp15 trimers form a, back-to-back hexamer that is believed to be the functional unit. The, structure reveals the catalytic site including the highly conserved, residues His262, His277, and Lys317, which is supported by mutagenesis, analysis. Gel filtration and enzyme activity assays confirmed that the, hexamer is the active form for nsp15 and demonstrate the specificity of, nsp15 for uridylate. The high sequence conservation of nsp15 in, coronaviruses, including that of severe acute respiratory syndrome, suggests that this protein may provide a new target for the design of, antiviral therapeutics.
About this StructureAbout this Structure
2GTH is a Single protein structure of sequence from Murine hepatitis virus. Full crystallographic information is available from OCA.
ReferenceReference
New antiviral target revealed by the hexameric structure of mouse hepatitis virus nonstructural protein nsp15., Xu X, Zhai Y, Sun F, Lou Z, Su D, Xu Y, Zhang R, Joachimiak A, Zhang XC, Bartlam M, Rao Z, J Virol. 2006 Aug;80(16):7909-17. PMID:16873248
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