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- PDB-6of7: Crystal structure of the CRY1-PER2 complex -

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Basic information

Entry
Database: PDB / ID: 6of7
TitleCrystal structure of the CRY1-PER2 complex
Components
  • Cryptochrome-1
  • Period circadian protein homolog 2
KeywordsCIRCADIAN 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
Period circadian-like, C-terminal / Period protein 2/3C-terminal region / DNA Cyclobutane Dipyrimidine Photolyase, subunit A; domain 3 / DNA Cyclobutane Dipyrimidine Photolyase, subunit A, domain 3 / Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat - #80 / Cryptochrome/DNA photolyase class 1 / Cryptochrome/DNA photolyase, FAD-binding domain / FAD binding domain of DNA photolyase / PAS fold-3 / PAS fold ...Period circadian-like, C-terminal / Period protein 2/3C-terminal region / DNA Cyclobutane Dipyrimidine Photolyase, subunit A; domain 3 / DNA Cyclobutane Dipyrimidine Photolyase, subunit A, domain 3 / Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat - #80 / Cryptochrome/DNA photolyase class 1 / Cryptochrome/DNA photolyase, FAD-binding domain / FAD binding domain of DNA photolyase / PAS fold-3 / PAS fold / DNA photolyase, N-terminal / Cryptochrome/photolyase, N-terminal domain superfamily / DNA photolyase / Photolyase/cryptochrome alpha/beta domain profile. / Cryptochrome/DNA photolyase, FAD-binding domain-like superfamily / HUPs / PAS domain / PAS repeat profile. / Rossmann-like alpha/beta/alpha sandwich fold / PAS domain / PAS domain superfamily / Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat / Alpha Horseshoe / Rossmann fold / Orthogonal Bundle / 3-Layer(aba) Sandwich / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
Period circadian protein homolog 2 / Cryptochrome-1
Similarity search - Component
Biological speciesMus musculus (house mouse)
Homo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.11 Å
AuthorsMichael, A.K. / Fribourgh, J.L. / Tripathi, S.M. / Partch, C.L.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)GM107069 United States
CitationJournal: 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
DepositionMar 28, 2019Deposition site: RCSB / Processing site: RCSB
Revision 1.0Mar 4, 2020Provider: repository / Type: Initial release
Revision 1.1Sep 16, 2020Group: Database references / Category: citation / citation_author
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year
Revision 1.2Oct 11, 2023Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Cryptochrome-1
B: Period circadian protein homolog 2


Theoretical massNumber of molelcules
Total (without water)71,1962
Polymers71,1962
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: fluorescence resonance energy transfer
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5230 Å2
ΔGint-38 kcal/mol
Surface area25260 Å2
MethodPISA
Unit cell
Length a, b, c (Å)72.640, 81.230, 98.100
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121

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Components

#1: Protein Cryptochrome-1 /


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
#2: Protein Period circadian protein homolog 2 / hPER2 / Circadian clock protein PERIOD 2


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

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 2.03 Å3/Da / Density % sol: 39.49 %
Crystal growTemperature: 295 K / Method: vapor diffusion, hanging drop
Details: 0.2 M magnesium chloride, 0.1 M Bis-Tris, pH 5.5, 25% PEG3350

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Data collection

DiffractionMean temperature: 75 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 23-ID-D / Wavelength: 1 Å
DetectorType: DECTRIS PILATUS3 S 6M / Detector: PIXEL / Date: Jul 6, 2016
RadiationMonochromator: double crystal cryo-cooled Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 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 shellResolution: 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

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Processing

Software
NameVersionClassification
PHENIX(1.13_2998: ???)refinement
MOSFLMdata reduction
Aimlessdata scaling
PHASERphasing
RefinementMethod 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
RfactorNum. reflection% reflection
Rfree0.2617 555 5.09 %
Rwork0.2084 --
obs0.2113 10898 99.92 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Refinement stepCycle: LAST / Resolution: 3.11→62.565 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4424 0 0 0 4424
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0024540
X-RAY DIFFRACTIONf_angle_d0.4286168
X-RAY DIFFRACTIONf_dihedral_angle_d1.8042704
X-RAY DIFFRACTIONf_chiral_restr0.037664
X-RAY DIFFRACTIONf_plane_restr0.003796
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3.11-3.4230.40671330.27252529X-RAY DIFFRACTION100
3.423-3.91820.28441310.22662549X-RAY DIFFRACTION100
3.9182-4.93620.22511180.18432596X-RAY DIFFRACTION100
4.9362-62.57810.23271730.19442669X-RAY DIFFRACTION100

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