1R7G
NMR structure of the membrane anchor domain (1-31) of the nonstructural protein 5A (NS5A) of hepatitis C virus (Minimized average structure, Sample in 100mM DPC)
Summary for 1R7G
| Entry DOI | 10.2210/pdb1r7g/pdb |
| Related | 1R7C 1R7D 1R7E 1R7F |
| NMR Information | BMRB: 5978 |
| Descriptor | Genome polyprotein (1 entity in total) |
| Functional Keywords | membrane anchor domain, hcv ns5a protein, peptide., membrane protein |
| Cellular location | Core protein p21: Host endoplasmic reticulum membrane; Single-pass membrane protein (By similarity). Core protein p19: Virion (By similarity). Envelope glycoprotein E1: Virion membrane; Single-pass type I membrane protein (Potential). Envelope glycoprotein E2: Virion membrane; Single-pass type I membrane protein (Potential). p7: Host endoplasmic reticulum membrane; Multi-pass membrane protein. Protease NS2-3: Host endoplasmic reticulum membrane; Multi-pass membrane protein (Potential). Serine protease NS3: Host endoplasmic reticulum membrane; Peripheral membrane protein (By similarity). Non-structural protein 4A: Host endoplasmic reticulum membrane; Single-pass type I membrane protein (Potential). Non-structural protein 4B: Host endoplasmic reticulum membrane; Multi-pass membrane protein. Non-structural protein 5A: Host endoplasmic reticulum membrane; Peripheral membrane protein. RNA-directed RNA polymerase: Host endoplasmic reticulum membrane; Single-pass type I membrane protein (Potential): P27958 |
| Total number of polymer chains | 1 |
| Total formula weight | 3770.42 |
| Authors | Penin, F.,Brass, V.,Appel, N.,Ramboarina, S.,Montserret, R.,Ficheux, D.,Blum, H.E.,Bartenschlager, R.,Moradpour, D. (deposition date: 2003-10-21, release date: 2004-08-10, Last modification date: 2024-05-22) |
| Primary citation | Penin, F.,Brass, V.,Appel, N.,Ramboarina, S.,Montserret, R.,Ficheux, D.,Blum, H.E.,Bartenschlager, R.,Moradpour, D. Structure and function of the membrane anchor domain of hepatitis C virus nonstructural protein 5A. J.Biol.Chem., 279:40835-40843, 2004 Cited by PubMed Abstract: Hepatitis C virus (HCV) nonstructural protein 5A (NS5A) is a membrane-associated, essential component of the viral replication complex. Here, we report the three-dimensional structure of the membrane anchor domain of NS5A as determined by NMR spectroscopy. An alpha-helix extending from amino acid residue 5 to 25 was observed in the presence of different membrane mimetic media. This helix exhibited a hydrophobic, Trprich side embedded in detergent micelles, while the polar, charged side was exposed to the solvent. Thus, the NS5A membrane anchor domain forms an in-plane amphipathic alpha-helix embedded in the cytosolic leaflet of the membrane bilayer. Interestingly, mutations affecting the positioning of fully conserved residues located at the cytosolic surface of the helix impaired HCV RNA replication without interfering with the membrane association of NS5A. In conclusion, the NS5A membrane anchor domain constitutes a unique platform that is likely involved in specific interactions essential for the assembly of the HCV replication complex and that may represent a novel target for antiviral intervention. PubMed: 15247283DOI: 10.1074/jbc.M404761200 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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