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- PDB-1r7f: NMR structure of the membrane anchor domain (1-31) of the nonstru... -
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Basic information
Entry | Database: PDB / ID: 1r7f | ||||||
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Title | NMR structure of the membrane anchor domain (1-31) of the nonstructural protein 5A (NS5A) of hepatitis C virus (Ensemble of 43 structures. Sample in 100mM SDS) | ||||||
![]() | Genome polyprotein | ||||||
![]() | MEMBRANE PROTEIN / Membrane anchor domain / HCV NS5A protein / peptide. | ||||||
Function / homology | ![]() positive regulation of hexokinase activity / modulation by virus of host cellular process / translocation of peptides or proteins into host cell cytoplasm / Toll-like receptor 2 binding / viral capsid assembly / adhesion receptor-mediated virion attachment to host cell / TBC/RABGAPs / hepacivirin / host cell mitochondrial membrane / host cell lipid droplet ...positive regulation of hexokinase activity / modulation by virus of host cellular process / translocation of peptides or proteins into host cell cytoplasm / Toll-like receptor 2 binding / viral capsid assembly / adhesion receptor-mediated virion attachment to host cell / TBC/RABGAPs / hepacivirin / host cell mitochondrial membrane / host cell lipid droplet / symbiont-mediated suppression of host TRAF-mediated signal transduction / transformation of host cell by virus / positive regulation of cytokinesis / symbiont-mediated perturbation of host cell cycle G1/S transition checkpoint / negative regulation of protein secretion / symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT1 activity / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of MAVS activity / endoplasmic reticulum-Golgi intermediate compartment membrane / kinase binding / SH3 domain binding / nucleoside-triphosphate phosphatase / protein complex oligomerization / monoatomic ion channel activity / viral nucleocapsid / clathrin-dependent endocytosis of virus by host cell / entry receptor-mediated virion attachment to host cell / Hydrolases; Acting on peptide bonds (peptidases); Cysteine endopeptidases / RNA helicase activity / host cell perinuclear region of cytoplasm / host cell endoplasmic reticulum membrane / symbiont-mediated suppression of host type I interferon-mediated signaling pathway / RNA helicase / ribonucleoprotein complex / induction by virus of host autophagy / RNA-directed RNA polymerase / viral RNA genome replication / cysteine-type endopeptidase activity / serine-type endopeptidase activity / RNA-dependent RNA polymerase activity / virus-mediated perturbation of host defense response / fusion of virus membrane with host endosome membrane / viral envelope / host cell nucleus / apoptotic process / host cell plasma membrane / structural molecule activity / virion membrane / negative regulation of transcription by RNA polymerase II / ATP hydrolysis activity / proteolysis / RNA binding / zinc ion binding / ATP binding Similarity search - Function | ||||||
Method | SOLUTION NMR / distance geometry, simulated annealing, molecular dynamics, energy minimization | ||||||
![]() | Penin, F. / Brass, V. / Appel, N. / Ramboarina, S. / Montserret, R. / Ficheux, D. / Blum, H.E. / Bartenschlager, R. / Moradpour, D. | ||||||
![]() | ![]() Title: Structure and function of the membrane anchor domain of hepatitis C virus nonstructural protein 5A. Authors: Penin, F. / Brass, V. / Appel, N. / Ramboarina, S. / Montserret, R. / Ficheux, D. / Blum, H.E. / Bartenschlager, R. / Moradpour, D. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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PDBx/mmCIF format | ![]() | 441.6 KB | Display | ![]() |
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PDB format | ![]() | 368.7 KB | Display | ![]() |
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-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein/peptide | Mass: 3770.423 Da / Num. of mol.: 1 Fragment: Nonstructural protein NS5A (P56)(residues 1973-2003 of Swiss-Prot sequence P27958) Source method: obtained synthetically Details: The peptide was chemically synthesized. The sequence is naturally found in hepatitis C virus. References: UniProt: P27958 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||
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NMR experiment |
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Sample preparation
Details | Contents: 1.2mM NS5A[1-31], 10mM DTTd10 / Solvent system: 100mM SDS in H2O/D2O 95/5 (v/v) |
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Sample conditions | pH: 6 / Pressure: ambient / Temperature: 313 K |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M |
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Radiation wavelength | Relative weight: 1 |
NMR spectrometer | Type: Varian UNITYPLUS / Manufacturer: Varian / Model: UNITYPLUS / Field strength: 500 MHz |
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Processing
NMR software |
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Refinement | Method: distance geometry, simulated annealing, molecular dynamics, energy minimization Software ordinal: 1 | ||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the least restraint violations Conformers calculated total number: 100 / Conformers submitted total number: 43 |