+Open data
-Basic information
Entry | Database: PDB / ID: 6of7 | ||||||
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Title | Crystal structure of the CRY1-PER2 complex | ||||||
Components |
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Keywords | CIRCADIAN CLOCK PROTEIN / Cryptochrome-1 / Period 2 complex | ||||||
Function / homology | Function and homology information regulation of glutamate uptake involved in transmission of nerve impulse / : / circadian regulation of translation / negative regulation of glucocorticoid secretion / negative regulation of fat cell proliferation / negative regulation of glucocorticoid receptor signaling pathway / negative regulation of transcription regulatory region DNA binding / negative regulation of circadian rhythm / lactate biosynthetic process / negative regulation of G protein-coupled receptor signaling pathway ...regulation of glutamate uptake involved in transmission of nerve impulse / : / circadian regulation of translation / negative regulation of glucocorticoid secretion / negative regulation of fat cell proliferation / negative regulation of glucocorticoid receptor signaling pathway / negative regulation of transcription regulatory region DNA binding / negative regulation of circadian rhythm / lactate biosynthetic process / negative regulation of G protein-coupled receptor signaling pathway / lipid storage / regulation of DNA damage checkpoint / glycogen biosynthetic process / response to glucagon / regulation of gluconeogenesis / entrainment of circadian clock by photoperiod / E-box binding / photoreceptor activity / regulation of insulin secretion / response to light stimulus / regulation of vasoconstriction / white fat cell differentiation / regulation of neurogenesis / phosphatase binding / negative regulation of gluconeogenesis / signal transduction in response to DNA damage / positive regulation of gluconeogenesis / negative regulation of protein ubiquitination / FAD binding / transcription corepressor binding / fatty acid metabolic process / response to activity / positive regulation of protein ubiquitination / response to ischemia / gluconeogenesis / nuclear receptor binding / circadian regulation of gene expression / response to insulin / regulation of circadian rhythm / kinase binding / circadian rhythm / histone deacetylase binding / Circadian Clock / glucose homeostasis / positive regulation of cold-induced thermogenesis / double-stranded DNA binding / DNA-binding transcription factor binding / transcription coactivator activity / transcription cis-regulatory region binding / regulation of cell cycle / negative regulation of DNA-templated transcription / nucleolus / protein kinase binding / perinuclear region of cytoplasm / negative regulation of transcription by RNA polymerase II / mitochondrion / DNA binding / nucleoplasm / nucleus / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Mus musculus (house mouse) Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.11 Å | ||||||
Authors | Michael, A.K. / Fribourgh, J.L. / Tripathi, S.M. / Partch, C.L. | ||||||
Funding support | United States, 1items
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Citation | Journal: Elife / Year: 2020 Title: Dynamics at the serine loop underlie differential affinity of cryptochromes for CLOCK:BMAL1 to control circadian timing. Authors: Fribourgh, J.L. / Srivastava, A. / Sandate, C.R. / Michael, A.K. / Hsu, P.L. / Rakers, C. / Nguyen, L.T. / Torgrimson, M.R. / Parico, G.C.G. / Tripathi, S. / Zheng, N. / Lander, G.C. / ...Authors: Fribourgh, J.L. / Srivastava, A. / Sandate, C.R. / Michael, A.K. / Hsu, P.L. / Rakers, C. / Nguyen, L.T. / Torgrimson, M.R. / Parico, G.C.G. / Tripathi, S. / Zheng, N. / Lander, G.C. / Hirota, T. / Tama, F. / Partch, C.L. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 6of7.cif.gz | 125.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6of7.ent.gz | 93.8 KB | Display | PDB format |
PDBx/mmJSON format | 6of7.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/of/6of7 ftp://data.pdbj.org/pub/pdb/validation_reports/of/6of7 | HTTPS FTP |
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-Related structure data
Related structure data | 4ct0S S: Starting model for refinement |
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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: 56591.879 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Gene: Cry1 / Production host: Escherichia coli (E. coli) / References: UniProt: P97784 |
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#2: Protein | Mass: 14604.450 Da / Num. of mol.: 1 / Fragment: UNP residues 1093-1212 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: PER2, KIAA0347 / Production host: Escherichia coli (E. coli) / References: UniProt: O15055 |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.03 Å3/Da / Density % sol: 39.49 % |
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Crystal grow | Temperature: 295 K / Method: vapor diffusion, hanging drop Details: 0.2 M magnesium chloride, 0.1 M Bis-Tris, pH 5.5, 25% PEG3350 |
-Data collection
Diffraction | Mean temperature: 75 K / Serial crystal experiment: N |
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Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 23-ID-D / Wavelength: 1 Å |
Detector | Type: DECTRIS PILATUS3 S 6M / Detector: PIXEL / Date: Jul 6, 2016 |
Radiation | Monochromator: double crystal cryo-cooled Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 3.11→62.565 Å / Num. obs: 10939 / % possible obs: 100 % / Redundancy: 5.8 % / CC1/2: 0.99 / Rmerge(I) obs: 0.17 / Net I/σ(I): 7.5 |
Reflection shell | Resolution: 3.11→3.28 Å / Redundancy: 6.1 % / Rmerge(I) obs: 0.65 / Mean I/σ(I) obs: 3 / Num. unique obs: 1564 / CC1/2: 0.75 / % possible all: 100 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB entry 4CT0 Resolution: 3.11→62.565 Å / SU ML: 0.43 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 26.87
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | |||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3.11→62.565 Å
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Refine LS restraints |
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LS refinement shell |
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