2L8K
NMR Structure of the Arterivirus nonstructural protein 7 alpha (nsp7 alpha)
Summary for 2L8K
| Entry DOI | 10.2210/pdb2l8k/pdb |
| NMR Information | BMRB: 16977 |
| Descriptor | Non-structural protein 7 (1 entity in total) |
| Functional Keywords | viral protein |
| Biological source | Equine arteritis virus (EAV) |
| Cellular location | Nsp1 papain-like cysteine proteinase: Host nucleus. Nsp2 cysteine proteinase: Host membrane; Multi-pass membrane protein (Potential). Non-structural protein 3: Host membrane; Multi-pass membrane protein (Potential). Non-structural protein 5-6-7: Host membrane; Multi-pass membrane protein (Potential). 3C-like serine proteinase: Host cytoplasm (Potential). RNA-directed RNA polymerase: Host cytoplasm, host perinuclear region (Potential). Helicase: Host cytoplasm, host perinuclear region (Potential): P19811 |
| Total number of polymer chains | 1 |
| Total formula weight | 13489.43 |
| Authors | Conte, M.R.,Gaudin, C.,Manolaridis, I.,Tucker, P.W.,Kelly, G. (deposition date: 2011-01-19, release date: 2011-07-06, Last modification date: 2024-05-15) |
| Primary citation | Manolaridis, I.,Gaudin, C.,Posthuma, C.C.,Zevenhoven-Dobbe, J.C.,Imbert, I.,Canard, B.,Kelly, G.,Tucker, P.A.,Conte, M.R.,Snijder, E.J. Structure and Genetic Analysis of the Arterivirus Nonstructural Protein 7{alpha}. J.Virol., 85:7449-7453, 2011 Cited by PubMed Abstract: Arterivirus replicase polyproteins are cleaved into at least 13 mature nonstructural proteins (nsps), and in particular the nsp5-to-nsp8 region is subject to a complex processing cascade. The function of the largest subunit from this region, nsp7, which is further cleaved into nsp7α and nsp7β, is unknown. Using nuclear magnetic resonance (NMR) spectroscopy, we determined the solution structure of nsp7α of equine arteritis virus, revealing an interesting unique fold for this protein but thereby providing little clue to its possible functions. Nevertheless, structure-based reverse genetics studies established the importance of nsp7/nsp7α for viral RNA synthesis, thus providing a basis for future studies. PubMed: 21561912DOI: 10.1128/JVI.00255-11 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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