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Open data
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Basic information
Entry | Database: PDB / ID: 5w0t | ||||||||||||||||||||||||
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Title | Crystal structure of monomeric Msp1 from S. cerevisiae | ||||||||||||||||||||||||
![]() | Protein MSP1 | ||||||||||||||||||||||||
![]() | HYDROLASE / AAA ATPase | ||||||||||||||||||||||||
Function / homology | ![]() extraction of mislocalized protein from mitochondrial outer membrane / Class I peroxisomal membrane protein import / membrane protein dislocase activity / Translocases; Catalysing the translocation of amino acids and peptides; Linked to the hydrolysis of a nucleoside triphosphate / protein targeting to mitochondrion / protein hexamerization / peroxisomal membrane / mitochondrial outer membrane / membrane => GO:0016020 / ATP hydrolysis activity ...extraction of mislocalized protein from mitochondrial outer membrane / Class I peroxisomal membrane protein import / membrane protein dislocase activity / Translocases; Catalysing the translocation of amino acids and peptides; Linked to the hydrolysis of a nucleoside triphosphate / protein targeting to mitochondrion / protein hexamerization / peroxisomal membrane / mitochondrial outer membrane / membrane => GO:0016020 / ATP hydrolysis activity / mitochondrion / ATP binding Similarity search - Function | ||||||||||||||||||||||||
Biological species | ![]() ![]() | ||||||||||||||||||||||||
Method | ![]() ![]() ![]() | ||||||||||||||||||||||||
![]() | Keenan, R.J. / Wohlever, M.L. / Mateja, A.M. | ||||||||||||||||||||||||
Funding support | ![]()
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![]() | ![]() Title: Msp1 Is a Membrane Protein Dislocase for Tail-Anchored Proteins. Authors: Wohlever, M.L. / Mateja, A. / McGilvray, P.T. / Day, K.J. / Keenan, R.J. #1: Journal: EMBO J. / Year: 2014 Title: Msp1/ATAD1 maintains mitochondrial function by facilitating the degradation of mislocalized tail-anchored proteins. Authors: Chen, Y.C. / Umanah, G.K. / Dephoure, N. / Andrabi, S.A. / Gygi, S.P. / Dawson, T.M. / Dawson, V.L. / Rutter, J. #2: Journal: Proc. Natl. Acad. Sci. U.S.A. / Year: 2014 Title: The conserved AAA-ATPase Msp1 confers organelle specificity to tail-anchored proteins. Authors: Okreglak, V. / Walter, P. #3: Journal: Cell / Year: 2011 Title: The AAA+ ATPase Thorase regulates AMPA receptor-dependent synaptic plasticity and behavior. Authors: Zhang, J. / Wang, Y. / Chi, Z. / Keuss, M.J. / Pai, Y.M. / Kang, H.C. / Shin, J.H. / Bugayenko, A. / Wang, H. / Xiong, Y. / Pletnikov, M.V. / Mattson, M.P. / Dawson, T.M. / Dawson, V.L. | ||||||||||||||||||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 133.4 KB | Display | ![]() |
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PDB format | ![]() | 109.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 439.2 KB | Display | ![]() |
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Full document | ![]() | 440.9 KB | Display | |
Data in XML | ![]() | 12.7 KB | Display | |
Data in CIF | ![]() | 16.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 34343.125 Da / Num. of mol.: 1 / Fragment: UNP residues 51-345 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: ATCC 204508 / S288c / Gene: MSP1, YTA4, YGR028W / Production host: ![]() ![]() | ||
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#2: Chemical | ChemComp-EDO / #3: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.76 Å3/Da / Density % sol: 55.41 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop Details: ~9 mg/ml protein in 20 mM Hepes pH 7.5, 100 mM NaCl and 1 mM DTT was mixed with reservoir solution containing 16% PEG3350 and 0.6 M Sodium Thiocyanate |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: PSI PILATUS 6M / Detector: PIXEL / Date: Oct 30, 2015 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97918 Å / Relative weight: 1 |
Reflection | Resolution: 2.63→206.71 Å / Num. obs: 11608 / % possible obs: 100 % / Redundancy: 17.4 % / CC1/2: 0.99 / Rmerge(I) obs: 0.211 / Rpim(I) all: 0.051 / Net I/σ(I): 9.9 |
Reflection shell | Resolution: 2.63→2.7 Å / Redundancy: 9.6 % / Rmerge(I) obs: 1.447 / Mean I/σ(I) obs: 1.2 / Num. unique obs: 843 / CC1/2: 0.762 / Rpim(I) all: 0.491 / % possible all: 100 |
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Processing
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Refinement | Method to determine structure: ![]()
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 261.93 Å2 / Biso mean: 76.4023 Å2 / Biso min: 40.07 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: final / Resolution: 2.63→68.902 Å
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Refine LS restraints |
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LS refinement shell | Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 4
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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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