2IDY

NMR Structure of the SARS-CoV non-structural protein nsp3a

2IDY の概要

• エントリーDOI: 10.2210/pdb2idy/pdb
• 関連するPDBエントリー: 2GRI
• NMR情報: BMRB: 7019
• 分子名称: NSP3 (1 entity in total)
• 機能のキーワード: sars coronavirus nmr nsp3a, structural genomics, psi-2, 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: 12648.01

構造登録者

Serrano, P.,Almeida, M.S.,Johnson, M.A.,Horst, R.,Herrmann, T.,Joseph, J.,Saikatendu, K.,Subramanian, V.,Stevens, R.C.,Kuhn, P.,Wuthrich, K.,Joint Center for Structural Genomics (JCSG) (登録日: 2006-09-15, 公開日: 2006-12-05, 最終更新日: 2024-05-29)

主引用文献

Serrano, P.,Johnson, M.A.,Almeida, M.S.,Horst, R.,Herrmann, T.,Joseph, J.S.,Neuman, B.W.,Subramanian, V.,Saikatendu, K.S.,Buchmeier, M.J.,Stevens, R.C.,Kuhn, P.,Wuthrich, K.
Nuclear magnetic resonance structure of the N-terminal domain of nonstructural protein 3 from the severe acute respiratory syndrome coronavirus.
J.Virol., 81:12049-12060, 2007

PubMed Abstract: This paper describes the structure determination of nsp3a, the N-terminal domain of the severe acute respiratory syndrome coronavirus (SARS-CoV) nonstructural protein 3. nsp3a exhibits a ubiquitin-like globular fold of residues 1 to 112 and a flexibly extended glutamic acid-rich domain of residues 113 to 183. In addition to the four beta-strands and two alpha-helices that are common to ubiquitin-like folds, the globular domain of nsp3a contains two short helices representing a feature that has not previously been observed in these proteins. Nuclear magnetic resonance chemical shift perturbations showed that these unique structural elements are involved in interactions with single-stranded RNA. Structural similarities with proteins involved in various cell-signaling pathways indicate possible roles of nsp3a in viral infection and persistence.

PubMed: 17728234
DOI: 10.1128/JVI.00969-07

実験手法

SOLUTION NMR