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- PDB-5bw8: 2.8 A crystal structure of a Get3-Get4-Get5 intermediate complex ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 5bw8 | ||||||
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Title | 2.8 A crystal structure of a Get3-Get4-Get5 intermediate complex from S.cerevisiae | ||||||
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![]() | Hydrolase/Transport / Tail-anchored targeting / ATPase / electrostatic interaction / Hydrolase-Transport complex | ||||||
Function / homology | ![]() cell morphogenesis involved in conjugation with cellular fusion / GET complex / pheromone-dependent signal transduction involved in conjugation with cellular fusion / TRC complex / tail-anchored membrane protein insertion into ER membrane / Hydrolases; Acting on acid anhydrides / protein insertion into ER membrane / post-translational protein targeting to endoplasmic reticulum membrane / response to arsenic-containing substance / retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum ...cell morphogenesis involved in conjugation with cellular fusion / GET complex / pheromone-dependent signal transduction involved in conjugation with cellular fusion / TRC complex / tail-anchored membrane protein insertion into ER membrane / Hydrolases; Acting on acid anhydrides / protein insertion into ER membrane / post-translational protein targeting to endoplasmic reticulum membrane / response to arsenic-containing substance / retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum / response to metal ion / protein folding chaperone / vesicle-mediated transport / guanyl-nucleotide exchange factor activity / cytoplasmic stress granule / unfolded protein binding / protein-folding chaperone binding / response to heat / endoplasmic reticulum membrane / Golgi apparatus / endoplasmic reticulum / ATP hydrolysis activity / ATP binding / identical protein binding / nucleus / metal ion binding / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Gristick, H.B. / Chartron, J.W. / Clemons, W.M. | ||||||
![]() | ![]() Title: Mechanism of Assembly of a Substrate Transfer Complex during Tail-anchored Protein Targeting. Authors: Gristick, H.B. / Rome, M.E. / Chartron, J.W. / Rao, M. / Hess, S. / Shan, S.O. / Clemons, W.M. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 391.1 KB | Display | ![]() |
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PDB format | ![]() | 321.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 476.4 KB | Display | ![]() |
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Full document | ![]() | 492.4 KB | Display | |
Data in XML | ![]() | 34.5 KB | Display | |
Data in CIF | ![]() | 47.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 5bwkC ![]() 3a37S ![]() 3lkuS 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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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments: Component-ID: _ / Ens-ID: 1 / Beg auth comp-ID: THR / Beg label comp-ID: THR / End auth comp-ID: ASP / End label comp-ID: ASP / Refine code: _ / Auth seq-ID: 4 - 352 / Label seq-ID: 23 - 371
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Components
#1: Protein | Mass: 41576.848 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: RM11-1a / Gene: GET3, SCRG_00595 / Production host: ![]() ![]() References: UniProt: B3LGZ3, UniProt: Q12154*PLUS, Hydrolases; Acting on acid anhydrides #2: Protein | | Mass: 35803.250 Da / Num. of mol.: 1 / Fragment: UNP residues 1-290 / Mutation: K258A, K260A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: ATCC 204508 / S288c / Gene: GET4, YOR164C, O3580 / Production host: ![]() ![]() #3: Protein | | Mass: 6034.042 Da / Num. of mol.: 1 / Fragment: UNP residues 1-54 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: ATCC 204508 / S288c / Gene: MDY2, GET5, TMA24, YOL111C / Production host: ![]() ![]() #4: Protein/peptide | | Mass: 1124.378 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Production host: ![]() ![]() #5: Chemical | ChemComp-ZN / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.76 Å3/Da / Density % sol: 55.47 % |
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Crystal grow | Temperature: 295 K / Method: vapor diffusion, sitting drop / Details: 17% PEG 3350, 0.24 M Na citrate, and 30 mM TCEP |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: PSI PILATUS 6M / Detector: PIXEL / Date: Feb 12, 2012 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.8→29.8 Å / Num. obs: 34114 / % possible obs: 97 % / Redundancy: 3.3 % / Rmerge(I) obs: 0.06 / Net I/σ(I): 8.3 |
Reflection shell | Resolution: 2.8→2.9 Å / Redundancy: 3.1 % / Rmerge(I) obs: 0.58 / Mean I/σ(I) obs: 1.6 / % possible all: 95.7 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 3A37 and 3LKU Resolution: 2.8→29.8 Å / Cor.coef. Fo:Fc: 0.945 / Cor.coef. Fo:Fc free: 0.922 / SU B: 39.837 / SU ML: 0.347 / Cross valid method: THROUGHOUT / ESU R: 1.562 / ESU R Free: 0.37 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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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: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 111.032 Å2
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Refinement step | Cycle: LAST / Resolution: 2.8→29.8 Å
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Refine LS restraints |
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