1FW5
SOLUTION STRUCTURE OF MEMBRANE BINDING PEPTIDE OF SEMLIKI FOREST VIRUS MRNA CAPPING ENZYME NSP1
Summary for 1FW5
| Entry DOI | 10.2210/pdb1fw5/pdb |
| Descriptor | NONSTRUCTURAL PROTEIN NSP1 (1 entity in total) |
| Functional Keywords | viral protein |
| Cellular location | Non-structural polyprotein: Host endosome membrane; Peripheral membrane protein; Cytoplasmic side. P123: Host endosome membrane; Peripheral membrane protein; Cytoplasmic side. mRNA-capping enzyme nsP1: Host endosome membrane; Peripheral membrane protein; Cytoplasmic side. Protease nsP2: Host endosome membrane; Peripheral membrane protein; Cytoplasmic side. Non-structural protein 3: Host endosome membrane; Peripheral membrane protein; Cytoplasmic side. RNA-directed RNA polymerase nsP4: Host endosome membrane; Peripheral membrane protein; Cytoplasmic side: P08411 |
| Total number of polymer chains | 1 |
| Total formula weight | 2334.67 |
| Authors | Lampio, A.,Kilpelinen, I.,Pesonen, S.,Karhi, K.,Auvinen, P.,Somerharju, P.,Kriinen, L. (deposition date: 2000-09-21, release date: 2001-09-21, Last modification date: 2024-05-22) |
| Primary citation | Lampio, A.,Kilpelainen, I.,Pesonen, S.,Karhi, K.,Auvinen, P.,Somerharju, P.,Kaariainen, L. Membrane binding mechanism of an RNA virus-capping enzyme. J.Biol.Chem., 275:37853-37859, 2001 Cited by PubMed Abstract: The RNA replication complex of Semliki Forest virus is bound to cytoplasmic membranes via the mRNA-capping enzyme Nsp1. Here we have studied the structure and liposome interactions of a synthetic peptide (245)GSTLYTESRKLLRSWHLPSV(264) corresponding to the membrane binding domain of Nsp1. The peptide interacted with liposomes only if negatively charged lipids were present that induced a structural change in the peptide from a random coil to a partially alpha-helical conformation. NMR structure shows that the alpha-helix is amphipathic, the hydrophobic surface consisting of several leucines, a valine, and a tryptophan moiety (Trp-259). Fluorescence studies revealed that this tryptophan intercalates in the bilayer to the depth of the ninth and tenth carbons of lipid acyl chains. Mutation W259A altered the mode of bilayer association of the peptide and abolished its ability to compete for membrane association of intact Nsp1, demonstrating its crucial role in the membrane association and function of Nsp1. PubMed: 10984480DOI: 10.1074/jbc.M004865200 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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