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Open data
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Basic information
Entry | Database: PDB / ID: 4brw | ||||||
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Title | Crystal structure of the yeast Dhh1-Pat1 complex | ||||||
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![]() | HYDROLASE / TRANSLATIONAL REPRESSION / MRNP REMODELING / P- BOD | ||||||
Function / homology | ![]() regulation of cytoplasmic mRNA processing body assembly / mRNA decay by 5' to 3' exoribonuclease / Lsm1-7-Pat1 complex / negative regulation of translational elongation / cytoplasmic side of membrane / deadenylation-dependent decapping of nuclear-transcribed mRNA / formation of translation preinitiation complex / P-body assembly / regulation of translational initiation / mRNA transport ...regulation of cytoplasmic mRNA processing body assembly / mRNA decay by 5' to 3' exoribonuclease / Lsm1-7-Pat1 complex / negative regulation of translational elongation / cytoplasmic side of membrane / deadenylation-dependent decapping of nuclear-transcribed mRNA / formation of translation preinitiation complex / P-body assembly / regulation of translational initiation / mRNA transport / stress granule assembly / negative regulation of translational initiation / positive regulation of translation / P-body / mRNA processing / kinetochore / cytoplasmic stress granule / cytosolic small ribosomal subunit / RNA helicase activity / negative regulation of translation / RNA helicase / cell cycle / cell division / mRNA binding / chromatin binding / ATP hydrolysis activity / RNA binding / ATP binding / nucleus / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Sharif, H. / Ozgur, S. / Sharma, K. / Basquin, C. / Urlaub, H. / Conti, E. | ||||||
![]() | ![]() Title: Structural Analysis of the Yeast Dhh1-Pat1 Complex Reveals How Dhh1 Engages Pat1, Edc3 and RNA in Mutually Exclusive Interactions Authors: Sharif, H. / Ozgur, S. / Sharma, K. / Basquin, C. / Urlaub, H. / Conti, E. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 94.6 KB | Display | ![]() |
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PDB format | ![]() | 70.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 458.6 KB | Display | ![]() |
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Full document | ![]() | 463.6 KB | Display | |
Data in XML | ![]() | 16.1 KB | Display | |
Data in CIF | ![]() | 20.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 4bruC ![]() 1s2mS C: citing same article ( S: Starting model for refinement |
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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: 42840.594 Da / Num. of mol.: 1 / Fragment: RESIDUES 46-422 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: S288C / Production host: ![]() ![]() |
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#2: Protein | Mass: 7912.046 Da / Num. of mol.: 1 / Fragment: N-TERMINAL DOMAIN RESIDUES 5-79 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: S288C / Production host: ![]() ![]() |
#3: Chemical | ChemComp-MPD / ( |
#4: Chemical | ChemComp-1PE / |
#5: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.21 Å3/Da / Density % sol: 61.74 % / Description: NONE |
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Crystal grow | Details: 50 MM TRIS PH 8.0, 4% MPD, 200 MM NACL, 25% PEG 400 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Feb 25, 2012 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97139 Å / Relative weight: 1 |
Reflection | Resolution: 2.8→79.88 Å / Num. obs: 17668 / % possible obs: 99.6 % / Redundancy: 8.6 % / Biso Wilson estimate: 73.29 Å2 / Rmerge(I) obs: 0.08 / Net I/σ(I): 18.3 |
Reflection shell | Resolution: 2.8→2.95 Å / Redundancy: 8.4 % / Rmerge(I) obs: 0.76 / Mean I/σ(I) obs: 2.8 / % possible all: 97.1 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1S2M Resolution: 2.795→48.474 Å / SU ML: 0.41 / σ(F): 1.37 / Phase error: 25.94 / Stereochemistry target values: ML / Details: DISORDERED CHAIN B RESIDUES 5-24, 55-79
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Solvent computation | Shrinkage radii: 0.7 Å / VDW probe radii: 1 Å / Solvent model: FLAT BULK SOLVENT MODEL | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 48.3 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.795→48.474 Å
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Refine LS restraints |
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LS refinement shell |
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