2JXF
The solution structure of HCV NS4B(40-69)
Summary for 2JXF
| Entry DOI | 10.2210/pdb2jxf/pdb |
| NMR Information | BMRB: 15559 |
| Descriptor | Genome polyprotein (1 entity in total) |
| Functional Keywords | membrane associated segment, acetylation, apoptosis, atp-binding, capsid protein, cytoplasm, endoplasmic reticulum, envelope protein, fusion protein, glycoprotein, helicase, host-virus interaction, hydrolase, interferon antiviral system evasion, lipid droplet, lipoprotein, metal-binding, mitochondrion, multifunctional enzyme, nucleotide-binding, nucleotidyltransferase, nucleus, oncogene, palmitate, phosphoprotein, protease, ribonucleoprotein, rna replication, rna-binding, rna-directed rna polymerase, secreted, serine protease, sh3-binding, thiol protease, transcription, transcription regulation, transferase, transmembrane, ubl conjugation, viral nucleoprotein, virion, zinc, viral protein, 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 | 3601.12 |
| Authors | Montserret, R.,Penin, F. (deposition date: 2007-11-19, release date: 2008-11-25, Last modification date: 2024-05-15) |
| Primary citation | Gouttenoire, J.,Castet, V.,Montserret, R.,Arora, N.,Raussens, V.,Ruysschaert, J.-M.,Diesis, E.,Blum, H.E.,Penin, F.,Moradpour, D. Identification of a Novel Determinant for Membrane Association in Hepatitis C Virus Nonstructural Protein 4B J.Virol., 83:6257-6268, 2009 Cited by PubMed Abstract: Nonstructural protein 4B (NS4B) plays an essential role in the formation of the hepatitis C virus (HCV) replication complex. It is a relatively poorly characterized integral membrane protein predicted to comprise four transmembrane segments in its central portion. Here, we describe a novel determinant for membrane association represented by amino acids (aa) 40 to 69 in the N-terminal portion of NS4B. This segment was sufficient to target and tightly anchor the green fluorescent protein to cellular membranes, as assessed by fluorescence microscopy as well as membrane extraction and flotation analyses. Circular dichroism and nuclear magnetic resonance structural analyses showed that this segment comprises an amphipathic alpha-helix extending from aa 42 to 66. Attenuated total reflection infrared spectroscopy and glycosylation acceptor site tagging revealed that this amphipathic alpha-helix has the potential to traverse the phospholipid bilayer as a transmembrane segment, likely upon oligomerization. Alanine substitution of the fully conserved aromatic residues on the hydrophobic helix side abrogated membrane association of the segment comprising aa 40 to 69 and disrupted the formation of a functional replication complex. These results provide the first atomic resolution structure of an essential membrane-associated determinant of HCV NS4B. PubMed: 19357161DOI: 10.1128/JVI.02663-08 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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