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Yorodumi- PDB-1hx6: P3, THE MAJOR COAT PROTEIN OF THE LIPID-CONTAINING BACTERIOPHAGE PRD1. -
+Open data
-Basic information
Entry | Database: PDB / ID: 1hx6 | ||||||
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Title | P3, THE MAJOR COAT PROTEIN OF THE LIPID-CONTAINING BACTERIOPHAGE PRD1. | ||||||
Components | MAJOR CAPSID PROTEIN | ||||||
Keywords | VIRAL PROTEIN / bacteriophage PRD1 / coat protein / jelly roll / viral beta barrel | ||||||
Function / homology | Function and homology information | ||||||
Biological species | Enterobacteria phage PRD1 (virus) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.65 Å | ||||||
Authors | Benson, S.D. / Bamford, J.K.H. / Bamford, D.H. / Burnett, R.M. | ||||||
Citation | Journal: Acta Crystallogr D Biol Crystallogr / Year: 2002 Title: The X-ray crystal structure of P3, the major coat protein of the lipid-containing bacteriophage PRD1, at 1.65 A resolution. Authors: Stacy D Benson / Jaana K H Bamford / Dennis H Bamford / Roger M Burnett / Abstract: P3 has been imaged with X-ray crystallography to reveal a trimeric molecule with strikingly similar characteristics to hexon, the major coat protein of adenovirus. The structure of native P3 has now ...P3 has been imaged with X-ray crystallography to reveal a trimeric molecule with strikingly similar characteristics to hexon, the major coat protein of adenovirus. The structure of native P3 has now been extended to 1.65 A resolution (R(work) = 19.0% and R(free) = 20.8%). The new high-resolution model shows that P3 forms crystals through hydrophobic patches solvated by 2-methyl-2,4-pentanediol molecules. It reveals details of how the molecule's high stability may be achieved through ordered solvent in addition to intra- and intersubunit interactions. Of particular importance is a 'puddle' at the top of the molecule containing a four-layer deep hydration shell that cross-links a complex structural feature formed by 'trimerization loops'. These loops also link subunits by extending over a neighbor to reach the third subunit in the trimer. As each subunit has two eight-stranded viral jelly rolls, the trimer has a pseudo-hexagonal shape to allow close packing in its 240 hexavalent capsid positions. Flexible regions in P3 facilitate these interactions within the capsid and with the underlying membrane. A selenometh-ionine P3 derivative, with which the structure was solved, has been refined to 2.2 A resolution (R(work) = 20.1% and R(free) = 22.8%). The derivatized molecule is essentially unchanged, although synchrotron radiation has the curious effect of causing it to rotate about its threefold axis. P3 is a second example of a trimeric 'double-barrel' protein that forms a stable building block with optimal shape for constructing a large icosahedral viral capsid. A major difference is that hexon has long variable loops that distinguish different adenovirus species. The short loops in P3 and the severe constraints of its various interactions explain why the PRD1 family has highly conserved coat proteins. #1: Journal: Cell(Cambridge,Mass.) / Year: 1999 Title: Viral Evolution Revealed by Bacteriophage PRD1 and Human Adenovirus Coat Protein Structures Authors: Benson, S.D. / Bamford, J.K. / Bamford, D.H. / Burnett, R.M. #2: Journal: J.Mol.Biol. / Year: 1993 Title: Crystallization of the Major Coat Protein of PRD1, a Bacteriophage with an Internal Membrane Authors: Stewart, P.L. / Ghosh, S. / Bamford, D.H. / Burnett, R.M. #3: Journal: Virology / Year: 1990 Title: Capsomer Proteins of Bacteriophage PRD1, a Bacterial Virus with a Membrane Authors: Bamford, J.K. / Bamford, D.H. #4: Journal: MOL.THER. / Year: 2000 Title: Type-specific Epitope Locations Revealed by X-ray Crystallographic Study of Adenovirus Type 5 Hexon Authors: Rux, J.J. / Burnett, R.M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1hx6.cif.gz | 254.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1hx6.ent.gz | 206.5 KB | Display | PDB format |
PDBx/mmJSON format | 1hx6.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1hx6_validation.pdf.gz | 478 KB | Display | wwPDB validaton report |
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Full document | 1hx6_full_validation.pdf.gz | 498.9 KB | Display | |
Data in XML | 1hx6_validation.xml.gz | 50.2 KB | Display | |
Data in CIF | 1hx6_validation.cif.gz | 73.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/hx/1hx6 ftp://data.pdbj.org/pub/pdb/validation_reports/hx/1hx6 | HTTPS FTP |
-Related structure data
Related structure data | 1hqnSC S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 43346.219 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Enterobacteria phage PRD1 (virus) / Genus: Tectivirus / Production host: Salmonella typhimurium (bacteria) / Strain (production host): DS88 / References: UniProt: P22535 #2: Chemical | #3: Chemical | ChemComp-NA / #4: Chemical | ChemComp-MPD / ( #5: 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: 3.48 Å3/Da / Density % sol: 64.4 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 4.2 Details: 30% MPD, 0.1 M sodium acetate, 0.2 M NaCl, pH 4.2, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: NSLS / Beamline: X12C / Wavelength: 0.95 Å |
Detector | Type: BRANDEIS / Detector: CCD / Date: Jun 11, 1997 / Details: mirrors |
Radiation | Monochromator: SI(III) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.95 Å / Relative weight: 1 |
Reflection | Resolution: 1.6→87 Å / Num. obs: 195631 / % possible obs: 94.2 % / Observed criterion σ(I): 2 / Redundancy: 4.6 % / Biso Wilson estimate: 17.7 Å2 / Rsym value: 4.7 / Net I/σ(I): 20 |
Reflection shell | Resolution: 1.65→1.69 Å / Redundancy: 1.5 % / Num. unique all: 8530 / Rsym value: 40.3 / % possible all: 61.2 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: selenomethionine P3 - PDB entry 1HQN Resolution: 1.65→53.45 Å / Rfactor Rfree error: 0.005 / Data cutoff high absF: 360397.3 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber / Details: maximum likelihood
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 48.85 Å2 / ksol: 0.332 e/Å3 | ||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 27 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 1.65→53.45 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.65→1.71 Å / Rfactor Rfree error: 0.026 / Total num. of bins used: 10
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Xplor file |
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