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- PDB-2jzw: How the HIV-1 nucleocapsid protein binds and destabilises the (-)... -

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Basic information

Entry
Database: PDB / ID: 2jzw
TitleHow the HIV-1 nucleocapsid protein binds and destabilises the (-)primer binding site during reverse transcription
Components
  • DNA (5'-D(*DGP*DTP*DCP*DCP*DCP*DTP*DGP*DTP*DTP*DCP*DGP*DGP*DGP*DC)-3')
  • HIV-1 nucleocapsid protein NCp7(12-55)
KeywordsVIRAL PROTEIN/DNA / human immunodeficiency virus type 1 (HIV-1) / nuclear magnetic resonance (NMR) / nucleocapsid protein (NCp7) / primer binding site (PBS) / exchange / VIRAL PROTEIN-DNA COMPLEX
Function / homology
Function and homology information


HIV-1 retropepsin / : / retroviral ribonuclease H / exoribonuclease H / : / exoribonuclease H activity / host multivesicular body / DNA integration / viral genome integration into host DNA / RNA-directed DNA polymerase ...HIV-1 retropepsin / : / retroviral ribonuclease H / exoribonuclease H / : / exoribonuclease H activity / host multivesicular body / DNA integration / viral genome integration into host DNA / RNA-directed DNA polymerase / establishment of integrated proviral latency / viral penetration into host nucleus / RNA-directed DNA polymerase activity / Transferases; Transferring phosphorus-containing groups; Nucleotidyltransferases / RNA-DNA hybrid ribonuclease activity / viral nucleocapsid / DNA recombination / Hydrolases; Acting on ester bonds / DNA-directed DNA polymerase / aspartic-type endopeptidase activity / DNA-directed DNA polymerase activity / symbiont entry into host cell / symbiont-mediated suppression of host gene expression / lipid binding / host cell nucleus / structural molecule activity / host cell plasma membrane / virion membrane / proteolysis / DNA binding / RNA binding / zinc ion binding / membrane
Similarity search - Function
Zinc finger, CCHC-type / HIV-1 Nucleocapsid Protein / Reverse transcriptase connection / Reverse transcriptase connection domain / Reverse transcriptase thumb / Reverse transcriptase thumb domain / Integrase Zinc binding domain / Zinc finger integrase-type profile. / Integrase-like, N-terminal / Integrase DNA binding domain ...Zinc finger, CCHC-type / HIV-1 Nucleocapsid Protein / Reverse transcriptase connection / Reverse transcriptase connection domain / Reverse transcriptase thumb / Reverse transcriptase thumb domain / Integrase Zinc binding domain / Zinc finger integrase-type profile. / Integrase-like, N-terminal / Integrase DNA binding domain / Integrase, C-terminal domain superfamily, retroviral / Integrase, N-terminal zinc-binding domain / Integrase, C-terminal, retroviral / Integrase DNA binding domain profile. / Immunodeficiency lentiviral matrix, N-terminal / gag gene protein p17 (matrix protein) / RNase H / Integrase core domain / Integrase, catalytic core / Integrase catalytic domain profile. / Retroviral nucleocapsid Gag protein p24, C-terminal domain / Gag protein p24 C-terminal domain / Retropepsin-like catalytic domain / Matrix protein, lentiviral and alpha-retroviral, N-terminal / Ribonuclease H domain / RNase H type-1 domain profile. / Reverse transcriptase (RNA-dependent DNA polymerase) / Reverse transcriptase domain / Reverse transcriptase (RT) catalytic domain profile. / Retropepsins / Retroviral aspartyl protease / Aspartyl protease, retroviral-type family profile. / Peptidase A2A, retrovirus, catalytic / Retrovirus capsid, C-terminal / Retroviral matrix protein / Few Secondary Structures / Irregular / Retrovirus capsid, N-terminal / zinc finger / Zinc knuckle / Zinc finger, CCHC-type superfamily / Zinc finger, CCHC-type / Zinc finger CCHC-type profile. / Ribonuclease H superfamily / Aspartic peptidase, active site / Eukaryotic and viral aspartyl proteases active site. / Aspartic peptidase domain superfamily / Ribonuclease H-like superfamily / Reverse transcriptase/Diguanylate cyclase domain / DNA/RNA polymerase superfamily
Similarity search - Domain/homology
DNA / DNA (> 10) / Gag-Pol polyprotein
Similarity search - Component
MethodSOLUTION NMR / simulated annealing
AuthorsBourbigot, S. / Ramalanjaona, N. / Salgado, G.F.J. / Mely, Y. / Roques, B.P. / Bouaziz, S. / Morellet, N.
CitationJournal: J.Mol.Biol. / Year: 2008
Title: How the HIV-1 nucleocapsid protein binds and destabilises the (-)primer binding site during reverse transcription.
Authors: Bourbigot, S. / Ramalanjaona, N. / Boudier, C. / Salgado, G.F. / Roques, B.P. / Mely, Y. / Bouaziz, S. / Morellet, N.
History
DepositionJan 21, 2008Deposition site: BMRB / Processing site: RCSB
Revision 1.0Jan 13, 2009Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Mar 16, 2022Group: Data collection / Database references / Derived calculations
Category: database_2 / pdbx_nmr_software ...database_2 / pdbx_nmr_software / pdbx_nmr_spectrometer / pdbx_struct_assembly / pdbx_struct_oper_list / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_nmr_software.name / _pdbx_nmr_spectrometer.model / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: HIV-1 nucleocapsid protein NCp7(12-55)
B: DNA (5'-D(*DGP*DTP*DCP*DCP*DCP*DTP*DGP*DTP*DTP*DCP*DGP*DGP*DGP*DC)-3')
hetero molecules


Theoretical massNumber of molelcules
Total (without water)9,4174
Polymers9,2872
Non-polymers1312
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)19 / 100structures with the least restraint violations,structures with the lowest energy
RepresentativeModel #1closest to the average

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Components

#1: Protein/peptide HIV-1 nucleocapsid protein NCp7(12-55)


Mass: 5022.822 Da / Num. of mol.: 1 / Source method: obtained synthetically / References: UniProt: P03366*PLUS
#2: DNA chain DNA (5'-D(*DGP*DTP*DCP*DCP*DCP*DTP*DGP*DTP*DTP*DCP*DGP*DGP*DGP*DC)-3')


Mass: 4263.751 Da / Num. of mol.: 1 / Source method: obtained synthetically / Details: HIV-1 primer binding site PBS
#3: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Zn

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1112D 1H-1H NOESY
1212D 1H-1H TOCSY
1312D DQF-COSY

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Sample preparation

DetailsContents: 1 mM NCp7(12-55), 1 mM P(-)PBS, 3 mM ZnCl2, 30 mM sodium chloride, 0.2 mM MgCl2, 90% H2O/10% D2O
Solvent system: 90% H2O/10% D2O
Sample
Conc. (mg/ml)ComponentSolution-ID
1 mMNCp7(12-55)1
1 mMP(-)PBS1
3 mMZnCl21
30 mMsodium chloride1
0.2 mMMgCl21
Sample conditionsIonic strength: 30 / pH: 6.5 / Pressure: ambient / Temperature: 293 K

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NMR measurement

NMR spectrometerType: Bruker Avance / Manufacturer: Bruker / Model: AVANCE / Field strength: 600 MHz

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Processing

NMR software
NameVersionDeveloperClassification
XwinNMR3Bruker Biospincollection
XwinNMR3Bruker Biospinprocessing
Discover2.98Accelrysrefinement
RefinementMethod: simulated annealing / Software ordinal: 1
NMR constraintsNOE constraints total: 710 / NOE intraresidue total count: 266 / NOE long range total count: 108 / NOE medium range total count: 72 / NOE sequential total count: 196
NMR representativeSelection criteria: closest to the average
NMR ensembleConformer selection criteria: structures with the least restraint violations,structures with the lowest energy
Conformers calculated total number: 100 / Conformers submitted total number: 19
NMR ensemble rmsDistance rms dev: 0.028 Å / Distance rms dev error: 0.006 Å

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