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Yorodumi- PDB-2a8r: 2.45 Angstrom Crystal Structure of the Complex Between the Nuclea... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2a8r | ||||||
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Title | 2.45 Angstrom Crystal Structure of the Complex Between the Nuclear SnoRNA Decapping Nudix Hydrolase X29 and Manganese in the Presence of 7-methyl-GTP | ||||||
Components | U8 snoRNA-binding protein X29 | ||||||
Keywords | TRANSLATION / HYDROLASE / modified nudix hydrolase fold | ||||||
Function / homology | Function and homology information inosine diphosphate phosphatase / sno(s)RNA catabolic process / dIDP phosphatase activity / dITP catabolic process / IDP phosphatase activity / positive regulation of cell cycle process / RNA NAD+-cap (NAD+-forming) hydrolase activity / dITP diphosphatase activity / negative regulation of rRNA processing / NAD-cap decapping ...inosine diphosphate phosphatase / sno(s)RNA catabolic process / dIDP phosphatase activity / dITP catabolic process / IDP phosphatase activity / positive regulation of cell cycle process / RNA NAD+-cap (NAD+-forming) hydrolase activity / dITP diphosphatase activity / negative regulation of rRNA processing / NAD-cap decapping / 5'-(N7-methylguanosine 5'-triphospho)-[mRNA] hydrolase / 5'-(N(7)-methylguanosine 5'-triphospho)-[mRNA] hydrolase activity / metalloexopeptidase activity / cobalt ion binding / snoRNA binding / mRNA catabolic process / manganese ion binding / nucleotide binding / mRNA binding / nucleolus / magnesium ion binding / protein homodimerization activity / nucleoplasm / nucleus / cytoplasm Similarity search - Function | ||||||
Biological species | Xenopus laevis (African clawed frog) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2.45 Å | ||||||
Authors | Scarsdale, J.N. / Peculis, B.A. / Wright, H.T. | ||||||
Citation | Journal: Structure / Year: 2006 Title: Crystal structures of U8 snoRNA decapping nudix hydrolase, X29, and its metal and cap complexes Authors: Scarsdale, J.N. / Peculis, B.A. / Wright, H.T. #1: Journal: Acta Crystallogr.,Sect.D / Year: 2004 Title: Crystals of X29, a Xenopus Laevis U8 SnoRNA Binding Protein with Nuclear Decapping Activity Authors: Peculis, B.A. / Scarsdale, J.N. / Wright, H.T. #2: Journal: Mol.Cell / Year: 2004 Title: Xenopus U8 SnoRNA Binding Protein is a Conserved Nuclear Decapping Enzyme Authors: Ghosh, T. / Peterson, B. / Tomasevic, N. / Peculis, B.A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2a8r.cif.gz | 92.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2a8r.ent.gz | 68.5 KB | Display | PDB format |
PDBx/mmJSON format | 2a8r.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/a8/2a8r ftp://data.pdbj.org/pub/pdb/validation_reports/a8/2a8r | HTTPS FTP |
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-Related structure data
Related structure data | 2a8pC 2a8qC 2a8sC 2a8tC 1u20S 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: 24504.127 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Xenopus laevis (African clawed frog) / Plasmid: pET19b / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DES)pLysS References: UniProt: Q569R2, UniProt: Q6TEC1*PLUS, Hydrolases; Acting on acid anhydrides; In phosphorus-containing anhydrides #2: Chemical | ChemComp-MN / #3: Chemical | #4: 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: 2.27 Å3/Da / Density % sol: 45.3 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 7.68 Details: 4-5 mg/ml X29, 0.025M HEPES pH 7.68, 3/75% PEG 6000, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU / Wavelength: 1.5418 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Detector | Type: RIGAKU RAXIS IIC / Detector: IMAGE PLATE / Date: Apr 14, 2004 / Details: Osmic Confocal Optics | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation | Monochromator: Osmic Confocal Optics / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection | Redundancy: 3.46 % / Av σ(I) over netI: 14.1 / Number: 754 / Rmerge(I) obs: 0.046 / Χ2: 0.99 / D res high: 2.45 Å / D res low: 23.51 Å / Num. obs: 17613 / % possible obs: 99.4 / Rejects: 460 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Diffraction reflection shell |
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Reflection | Resolution: 2.45→23.51 Å / Num. all: 17716 / Num. obs: 17613 / % possible obs: 99.4 % / Redundancy: 3.46 % / Rmerge(I) obs: 0.046 / Net I/σ(I): 14.1 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection shell | Resolution: 2.45→2.54 Å / Redundancy: 3.48 % / Rmerge(I) obs: 0.365 / Mean I/σ(I) obs: 3.1 / Num. unique all: 1727 / % possible all: 99.5 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB entry 1U20 Resolution: 2.45→23 Å / Cor.coef. Fo:Fc: 0.945 / Cor.coef. Fo:Fc free: 0.926 / SU B: 19.678 / SU ML: 0.217 / TLS residual ADP flag: LIKELY RESIDUAL Isotropic thermal model: TLS refinement followd by restrained refinement of individual B factors Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.507 / ESU R Free: 0.292 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: Simulated annealing via Torsion Angle Dynamics in CNS v1.0 was followed by refinement with REFMAC5,
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: BABINET MODEL WITH MASK | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 63.01 Å2
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Refine analyze | Luzzati coordinate error obs: 0.448 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.45→23 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.45→2.513 Å / Total num. of bins used: 20
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Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group | Refine-ID: X-RAY DIFFRACTION / Selection: ALL
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