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Yorodumi- PDB-1jva: CRYSTAL STRUCTURE OF THE VMA1-DERIVED ENDONUCLEASE BEARING THE N ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1jva | ||||||
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Title | CRYSTAL STRUCTURE OF THE VMA1-DERIVED ENDONUCLEASE BEARING THE N AND C EXTEIN PROPEPTIDES | ||||||
Components | VMA1-DERIVED HOMING ENDONUCLEASE X10SSS | ||||||
Keywords | HYDROLASE / PROTEIN-SPLICING / VMA1-DERIVED ENDONUCLEASE / INTEIN / THIAZOLIDINE INTERMEDIATE / VDE | ||||||
Function / homology | Function and homology information Insulin receptor recycling / Transferrin endocytosis and recycling / ROS and RNS production in phagocytes / Amino acids regulate mTORC1 / Golgi lumen acidification / vacuolar proton-transporting V-type ATPase, V1 domain / endosomal lumen acidification / proton-transporting V-type ATPase complex / vacuolar proton-transporting V-type ATPase complex / vacuolar acidification ...Insulin receptor recycling / Transferrin endocytosis and recycling / ROS and RNS production in phagocytes / Amino acids regulate mTORC1 / Golgi lumen acidification / vacuolar proton-transporting V-type ATPase, V1 domain / endosomal lumen acidification / proton-transporting V-type ATPase complex / vacuolar proton-transporting V-type ATPase complex / vacuolar acidification / intron homing / protein metabolic process / intein-mediated protein splicing / fungal-type vacuole membrane / H+-transporting two-sector ATPase / proton-transporting ATPase activity, rotational mechanism / proton transmembrane transport / proton-transporting ATP synthase activity, rotational mechanism / endonuclease activity / Hydrolases; Acting on ester bonds / Golgi membrane / mRNA binding / DNA binding / ATP binding Similarity search - Function | ||||||
Biological species | Saccharomyces cerevisiae (brewer's yeast) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.1 Å | ||||||
Authors | Mizutani, R. / Satow, Y. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2002 Title: Protein-splicing reaction via a thiazolidine intermediate: crystal structure of the VMA1-derived endonuclease bearing the N and C-terminal propeptides. Authors: Mizutani, R. / Nogami, S. / Kawasaki, M. / Ohya, Y. / Anraku, Y. / Satow, Y. #1: Journal: J.Biol.Chem. / Year: 1990 Title: Molecular structure of a gene, VMA1, encoding the catalytic subunit of H(+)-translocating adenosine triphosphatase from vacuolar membranes of Saccharomyces cerevisiae Authors: Hirata, R. / Ohsumi, Y. / Nakano, A. / Kawasaki, H. / Suzuki, K. / Anraku, Y. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1jva.cif.gz | 179.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1jva.ent.gz | 143.1 KB | Display | PDB format |
PDBx/mmJSON format | 1jva.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/jv/1jva ftp://data.pdbj.org/pub/pdb/validation_reports/jv/1jva | HTTPS FTP |
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-Related structure data
Related structure data | 1vdeS 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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Details | VDE exists as a monomer in solution. |
-Components
#1: Protein | Mass: 53150.145 Da / Num. of mol.: 2 / Fragment: RESIDUES 274-747 / Mutation: C284S/H362N/N737S/C738S Source method: isolated from a genetically manipulated source Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast) Gene: VMA1 / Plasmid: pET-17b-VDE-X10SSS / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: P17255, EC: 3.6.1.34 #2: 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: 2.39 Å3/Da / Density % sol: 48.4 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6.2 Details: PEG6000, BisTrisHCl, mercaptoethanol, magnesium chloride, cadmium chloride, pH 6.2, VAPOR DIFFUSION, HANGING DROP, temperature 293K | ||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 20 ℃ | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 110 K |
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Diffraction source | Source: SYNCHROTRON / Site: SPring-8 / Beamline: BL40B2 / Wavelength: 0.7 Å |
Detector | Type: RIGAKU RAXIS IV++ / Detector: IMAGE PLATE / Date: Jan 1, 2000 Details: double crystal monochromator and bent-cylinder mirror |
Radiation | Monochromator: Si 111 / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.7 Å / Relative weight: 1 |
Reflection | Resolution: 2.1→30 Å / Num. all: 57103 / Num. obs: 51056 / % possible obs: 89.4 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0.5 / Redundancy: 2.39 % / Biso Wilson estimate: 20.12 Å2 / Rmerge(I) obs: 0.032 / Net I/σ(I): 30.6 |
Reflection shell | Resolution: 2.1→2.18 Å / Redundancy: 1.63 % / Rmerge(I) obs: 0.155 / Mean I/σ(I) obs: 2.63 / Num. unique all: 5699 / % possible all: 70.9 |
Reflection | *PLUS Lowest resolution: 30 Å / Num. measured all: 122186 / Rmerge(I) obs: 0.032 |
Reflection shell | *PLUS % possible obs: 70.9 % / Num. unique obs: 4038 / Rmerge(I) obs: 0.155 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1VDE Resolution: 2.1→30 Å / Isotropic thermal model: isotropic / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Displacement parameters | Biso mean: 25.3 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.1→30 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.1→2.18 Å / Total num. of bins used: 10
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Xplor file | Serial no: 1 / Param file: PROTEIN_REP.PARAM / Topol file: PROTEIN.TOP | ||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Lowest resolution: 30 Å / Rfactor all: 0.2 / Rfactor Rfree: 0.24 / Rfactor Rwork: 0.198 | ||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Rfactor Rfree: 0.2996 / Rfactor Rwork: 0.2474 |