2GTH

crystal structure of the wildtype MHV coronavirus non-structural protein nsp15

2GTH の概要

• エントリーDOI: 10.2210/pdb2gth/pdb
• 分子名称: Replicase polyprotein 1ab (2 entities in total)
• 機能のキーワード: mhv, nsp15, viral protein
• 由来する生物種: Murine hepatitis virus
• 細胞内の位置: Non-structural protein 3: Host membrane; Multi-pass membrane protein (Potential). Non-structural protein 4: Host membrane; Multi-pass membrane protein (Potential). Non-structural protein 6: Host membrane; Multi-pass membrane protein (Potential). Non-structural protein 7: Host cytoplasm, host perinuclear region (By similarity). Non-structural protein 8: Host cytoplasm, host perinuclear region (By similarity). Non-structural protein 9: Host cytoplasm, host perinuclear region (By similarity). Non-structural protein 10: Host cytoplasm, host perinuclear region (By similarity). Helicase: Host endoplasmic reticulum-Golgi intermediate compartment (Potential). Uridylate-specific endoribonuclease: Host cytoplasm, host perinuclear region (By similarity): P16342
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 41697.20

構造登録者

Xu, X.,Zhai, Y.,Sun, F.,Lou, Z.,Su, D.,Rao, Z. (登録日: 2006-04-28, 公開日: 2006-08-15, 最終更新日: 2024-11-13)

主引用文献

Xu, X.,Zhai, Y.,Sun, F.,Lou, Z.,Su, D.,Xu, Y.,Zhang, R.,Joachimiak, A.,Zhang, X.C.,Bartlam, M.,Rao, Z.
New Antiviral Target Revealed by the Hexameric Structure of Mouse Hepatitis Virus Nonstructural Protein nsp15
J.Virol., 80:7909-7917, 2006

PubMed Abstract: 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.

PubMed: 16873248
DOI: 10.1128/JVI.00525-06

実験手法

X-RAY DIFFRACTION (2.7 Å)