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Yorodumi- PDB-4r5p: Crystal structure of HIV-1 reverse transcriptase (RT) with DNA an... -
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-Basic information
Entry | Database: PDB / ID: 4r5p | |||||||||
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Title | Crystal structure of HIV-1 reverse transcriptase (RT) with DNA and a nucleoside triphosphate mimic alpha-carboxy nucleoside phosphonate inhibitor | |||||||||
Components |
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Keywords | TRANSFERASE / HYDROLASE/DNA/INHIBITOR / Zidovudine / RT-DNA complex / AIDS / DNA-directed DNA polymerase / RN lipoprotein / HIV / metal-binding / alpha-CNP / ribonuclease H / RNAse H / A-CNP / multifunctional enzyme / nucleotidyltransferase / RNA-directed polymerase / HYDROLASE-DNA-INHIBITOR complex | |||||||||
Function / homology | Function and homology information HIV-1 retropepsin / : / retroviral ribonuclease H / exoribonuclease H / : / exoribonuclease H activity / host multivesicular body / DNA integration / RNA-directed DNA polymerase / viral genome integration into host DNA ...HIV-1 retropepsin / : / retroviral ribonuclease H / exoribonuclease H / : / exoribonuclease H activity / host multivesicular body / DNA integration / RNA-directed DNA polymerase / viral genome integration into host DNA / viral penetration into host nucleus / establishment of integrated proviral latency / 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 | |||||||||
Biological species | Human immunodeficiency virus type 1 synthetic construct (others) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.894 Å | |||||||||
Authors | Das, K. / Martinez, S.E. / Arnold, E. | |||||||||
Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 2015 Title: Alpha-carboxy nucleoside phosphonates as universal nucleoside triphosphate mimics. Authors: Balzarini, J. / Das, K. / Bernatchez, J.A. / Martinez, S.E. / Ngure, M. / Keane, S. / Ford, A. / Maguire, N. / Mullins, N. / John, J. / Kim, Y. / Dehaen, W. / Vande Voorde, J. / Liekens, S. ...Authors: Balzarini, J. / Das, K. / Bernatchez, J.A. / Martinez, S.E. / Ngure, M. / Keane, S. / Ford, A. / Maguire, N. / Mullins, N. / John, J. / Kim, Y. / Dehaen, W. / Vande Voorde, J. / Liekens, S. / Naesens, L. / Gotte, M. / Maguire, A.R. / Arnold, E. #1: Journal: Nat.Struct.Mol.Biol. / Year: 2012 Title: HIV-1 reverse transcriptase complex with DNA and nevirapine reveals non-nucleoside inhibition mechanism. Authors: Das, K. / Martinez, S.E. / Bauman, J.D. / Arnold, E. #2: Journal: J.Biol.Chem. / Year: 2009 Title: Structural basis for the role of the K65R mutation in HIV-1 reverse transcriptase polymerization, excision antagonism, and tenofovir resistance. Authors: Das, K. / Bandwar, R.P. / White, K.L. / Feng, J.Y. / Sarafianos, S.G. / Tuske, S. / Tu, X. / Clark, A.D. / Boyer, P.L. / Hou, X. / Gaffney, B.L. / Jones, R.A. / Miller, M.D. / Hughes, S.H. / Arnold, E. #3: Journal: Nat.Struct.Mol.Biol. / Year: 2010 Title: Structural basis of HIV-1 resistance to AZT by excision. Authors: Tu, X. / Das, K. / Han, Q. / Bauman, J.D. / Clark, A.D. / Hou, X. / Frenkel, Y.V. / Gaffney, B.L. / Jones, R.A. / Boyer, P.L. / Hughes, S.H. / Sarafianos, S.G. / Arnold, E. #4: Journal: Proc.Natl.Acad.Sci.USA / Year: 2008 Title: High-resolution structures of HIV-1 reverse transcriptase/TMC278 complexes: strategic flexibility explains potency against resistance mutations. Authors: Das, K. / Bauman, J.D. / Clark, A.D. / Frenkel, Y.V. / Lewi, P.J. / Shatkin, A.J. / Hughes, S.H. / Arnold, E. #5: Journal: Nucleic Acids Res. / Year: 2014 Title: Structures of HIV-1 RT-RNA/DNA ternary complexes with dATP and nevirapine reveal conformational flexibility of RNA/DNA: insights into requirements for RNase H cleavage. Authors: Das, K. / Martinez, S.E. / Bandwar, R.P. / Arnold, E. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4r5p.cif.gz | 453.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4r5p.ent.gz | 362.7 KB | Display | PDB format |
PDBx/mmJSON format | 4r5p.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/r5/4r5p ftp://data.pdbj.org/pub/pdb/validation_reports/r5/4r5p | HTTPS FTP |
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-Related structure data
Related structure data | 3v4iS S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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-Components
-HIV-1 reverse transcriptase, ... , 2 types, 4 molecules ACBD
#1: Protein | Mass: 64022.414 Da / Num. of mol.: 2 / Fragment: UNP residues 600-1153 / Mutation: Q258C, C280S, D498N Source method: isolated from a genetically manipulated source Source: (gene. exp.) Human immunodeficiency virus type 1 / Gene: gag-pol / Production host: Escherichia coli (E. coli) References: UniProt: P03366, RNA-directed DNA polymerase, DNA-directed DNA polymerase, retroviral ribonuclease H, exoribonuclease H #2: Protein | Mass: 50039.488 Da / Num. of mol.: 2 / Fragment: UNP residues 600-1027 / Mutation: C280S Source method: isolated from a genetically manipulated source Source: (gene. exp.) Human immunodeficiency virus type 1 / Gene: gag-pol / Production host: Escherichia coli (E. coli) References: UniProt: P03366, RNA-directed DNA polymerase, DNA-directed DNA polymerase |
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-DNA chain , 2 types, 4 molecules TEPF
#3: DNA chain | Mass: 8392.398 Da / Num. of mol.: 2 / Source method: obtained synthetically / Details: Template DNA / Source: (synth.) synthetic construct (others) #4: DNA chain | Mass: 6490.267 Da / Num. of mol.: 2 / Source method: obtained synthetically / Details: Primer DNA / Source: (synth.) synthetic construct (others) |
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-Sugars , 1 types, 2 molecules
#5: Polysaccharide |
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-Non-polymers , 4 types, 15 molecules
#6: Chemical | ChemComp-MG / #7: Chemical | #8: Chemical | ChemComp-SO4 / | #9: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 3.24 Å3/Da / Density % sol: 62.06 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, sitting drop / pH: 7.2 Details: 10% PEG8000, 100 mM ammonium sulfate, 5% w/v sucrose, 5% w/v glycerol, 20 mM magnesium chloride, 50 mM Bis-Tris propane, pH 7.2, VAPOR DIFFUSION, SITTING DROP, temperature 277K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: CHESS / Beamline: F1 / Wavelength: 0.918 Å |
Detector | Type: ADSC QUANTUM 270 / Detector: CCD / Date: Oct 13, 2013 |
Radiation | Monochromator: Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.918 Å / Relative weight: 1 |
Reflection | Resolution: 2.894→50 Å / Num. all: 72420 / Num. obs: 72131 / % possible obs: 99.6 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -1 / Redundancy: 4 % / Rmerge(I) obs: 0.107 / Net I/σ(I): 8.9 |
Reflection shell | Resolution: 2.894→2.95 Å / Redundancy: 3.4 % / Rmerge(I) obs: 0.634 / Mean I/σ(I) obs: 1.85 / Num. unique all: 3540 / % possible all: 99.2 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 3V4I Resolution: 2.894→44.536 Å / SU ML: 0.4 / σ(F): 0 / Phase error: 26.39 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 1 Å / VDW probe radii: 1.2 Å / Solvent model: FLAT BULK SOLVENT MODEL | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.894→44.536 Å
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Refine LS restraints |
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LS refinement shell |
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