1YSY

NMR Structure of the nonstructural Protein 7 (nsP7) from the SARS CoronaVirus

1YSY の概要

• エントリーDOI: 10.2210/pdb1ysy/pdb
• 分子名称: Replicase polyprotein 1ab (pp1ab) (ORF1AB) (1 entity in total)
• 機能のキーワード: helix bundle, structural genomics, psi, protein structure initiative, joint center for structural genomics, jcsg, viral protein
• 由来する生物種: SARS coronavirus
• 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): P59641
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 9472.02

構造登録者

Peti, W.,Herrmann, T.,Johnson, M.A.,Kuhn, P.,Stevens, R.C.,Wuthrich, K.,Joint Center for Structural Genomics (JCSG) (登録日: 2005-02-09, 公開日: 2005-12-06, 最終更新日: 2024-05-22)

主引用文献

Peti, W.,Johnson, M.A.,Herrmann, T.,Neuman, B.W.,Buchmeier, M.J.,Nelson, M.,Joseph, J.,Page, R.,Stevens, R.C.,Kuhn, P.
Structural genomics of the severe acute respiratory syndrome coronavirus: nuclear magnetic resonance structure of the protein nsP7.
J.Virol., 79:12905-12913, 2005

PubMed Abstract: Here, we report the three-dimensional structure of severe acute respiratory syndrome coronavirus (SARS-CoV) nsP7, a component of the SARS-CoV replicase polyprotein. The coronavirus replicase carries out regulatory tasks involved in the maintenance, transcription, and replication of the coronavirus genome. nsP7 was found to assume a compact architecture in solution, which is comprised primarily of helical secondary structures. Three helices (alpha2 to alpha4) form a flat up-down-up antiparallel alpha-helix sheet. The N-terminal segment of residues 1 to 22, containing two turns of alpha-helix and one turn of 3(10)-helix, is packed across the surface of alpha2 and alpha3 in the helix sheet, with the alpha-helical region oriented at a 60 degrees angle relative to alpha2 and alpha3. The surface charge distribution is pronouncedly asymmetrical, with the flat surface of the helical sheet showing a large negatively charged region adjacent to a large hydrophobic patch and the opposite side containing a positively charged groove that extends along the helix alpha1. Each of these three areas is thus implicated as a potential site for protein-protein interactions.

PubMed: 16188992
DOI: 10.1128/JVI.79.20.12905-12913.2005

実験手法

SOLUTION NMR