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- PDB-2a8t: 2.1 Angstrom Crystal Structure of the Complex Between the Nuclear... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2a8t | ||||||
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Title | 2.1 Angstrom Crystal Structure of the Complex Between the Nuclear U8 snoRNA Decapping Nudix Hydrolase X29, Manganese and m7G-PPP-A | ||||||
![]() | U8 snoRNA-binding protein X29 | ||||||
![]() | TRANSLATION / HYDROLASE / modified nudix hydrolase fold | ||||||
Function / homology | ![]() 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 / phosphodiesterase decapping endonuclease activity / negative regulation of rRNA processing ...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 / phosphodiesterase decapping endonuclease 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 / snoRNA binding / cobalt ion 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 | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Scarsdale, J.N. / Peculis, B.A. / Wright, H.T. | ||||||
![]() | ![]() 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: ![]() 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: ![]() 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: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 95.3 KB | Display | ![]() |
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PDB format | ![]() | 71.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 2a8pC ![]() 2a8qC ![]() 2a8rC ![]() 2a8sC ![]() 1u20S S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 24390.025 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Details: complexed with N-methyl-Guanosine-triphosphate-Guanosine Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: Q569R2, UniProt: Q6TEC1*PLUS, Hydrolases; Acting on acid anhydrides; In phosphorus-containing anhydrides #2: Chemical | ChemComp-MN / #3: Chemical | #4: Chemical | #5: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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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 / 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: 95 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS IV / Detector: IMAGE PLATE / Date: Apr 3, 2005 / Details: OSMIC VARIMAX CONFOCAL OPTICS |
Radiation | Monochromator: OSMIC VARIMAX CONFOCAL OPTICS / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.1→46.17 Å / Num. obs: 27774 / % possible obs: 99.9 % / Redundancy: 6.92 % / Biso Wilson estimate: 57.6 Å2 / Rmerge(I) obs: 0.037 / Net I/σ(I): 19.8 |
Reflection shell | Resolution: 2.1→2.18 Å / Redundancy: 6.88 % / Rmerge(I) obs: 0.38 / Mean I/σ(I) obs: 4.4 / % possible all: 100 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1U20 Resolution: 2.1→46.17 Å / Cor.coef. Fo:Fc: 0.96 / Cor.coef. Fo:Fc free: 0.938 / SU B: 12.983 / SU ML: 0.164 / TLS residual ADP flag: LIKELY RESIDUAL Isotropic thermal model: TLS refinement followed by restrained refinement of individual isotropic B factors Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.232 / ESU R Free: 0.203 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: SIMULATED ANNEALING VIA TORSION ANGLE DYNAMICS IN CNS V1.0 WAS FOLLOWED BY MAXIMUM LIKELIHOOD REFINEMENT IN 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: 59.1 Å2
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Refine analyze | Luzzati coordinate error obs: 0.414 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.1→46.17 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.1→2.15 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 |
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