+Open data
-Basic information
Entry | Database: PDB / ID: 6lz7 | ||||||
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Title | Tetrameric structure of ZmCRY1a PHR domain | ||||||
Components | Cryptochrome-1 | ||||||
Keywords | PLANT PROTEIN / Cryptochrome / photoreceptor / photosignaling | ||||||
Function / homology | Function and homology information blue light photoreceptor activity / : / entrainment of circadian clock by photoperiod / FAD binding / circadian regulation of gene expression / DNA binding / nucleus / cytoplasm Similarity search - Function | ||||||
Biological species | Zea mays (maize) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.59936165826 Å | ||||||
Authors | Shao, K. / Zhang, X. / Zhang, P. | ||||||
Citation | Journal: Nat Struct Mol Biol / Year: 2020 Title: The oligomeric structures of plant cryptochromes. Authors: Kai Shao / Xue Zhang / Xu Li / Yahui Hao / Xiaowei Huang / Miaolian Ma / Minhua Zhang / Fang Yu / Hongtao Liu / Peng Zhang / Abstract: Cryptochromes (CRYs) are a group of evolutionarily conserved flavoproteins found in many organisms. In plants, the well-studied CRY photoreceptor, activated by blue light, plays essential roles in ...Cryptochromes (CRYs) are a group of evolutionarily conserved flavoproteins found in many organisms. In plants, the well-studied CRY photoreceptor, activated by blue light, plays essential roles in plant growth and development. However, the mechanism of activation remains largely unknown. Here, we determined the oligomeric structures of the blue-light-perceiving PHR domain of Zea mays CRY1 and an Arabidopsis CRY2 constitutively active mutant. The structures form dimers and tetramers whose functional importance is examined in vitro and in vivo with Arabidopsis CRY2. Structure-based analysis suggests that blue light may be perceived by CRY to cause conformational changes, whose precise nature remains to be determined, leading to oligomerization that is essential for downstream signaling. This photoactivation mechanism may be widely used by plant CRYs. Our study reveals a molecular mechanism of plant CRY activation and also paves the way for design of CRY as a more efficient optical switch. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 6lz7.cif.gz | 137.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6lz7.ent.gz | 87.3 KB | Display | PDB format |
PDBx/mmJSON format | 6lz7.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/lz/6lz7 ftp://data.pdbj.org/pub/pdb/validation_reports/lz/6lz7 | HTTPS FTP |
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-Related structure data
Related structure data | 6lz3C 1u3cS S: Starting model for refinement C: citing same article (ref.) |
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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: 57799.184 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Zea mays (maize) / Gene: 100384475, ZEAMMB73_Zm00001d016915 / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: A0A1D6HB66, UniProt: A0A1D6HB67*PLUS |
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#2: Chemical | ChemComp-FAD / |
Has ligand of interest | Y |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 4.27 Å3/Da / Density % sol: 71.18 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, sitting drop / Details: 20%(w/v) PEG 3350, 0.2M sodium thiocyanate |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: SYNCHROTRON / Site: NFPSS / Beamline: BL19U1 / Wavelength: 0.9785 Å |
Detector | Type: MAR555 FLAT PANEL / Detector: IMAGE PLATE / Date: Dec 1, 2018 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9785 Å / Relative weight: 1 |
Reflection | Resolution: 3.599→30.61 Å / Num. obs: 15933 / % possible obs: 99.9 % / Redundancy: 15.1 % / Biso Wilson estimate: 63.1281446645 Å2 / CC1/2: 0.99 / Net I/σ(I): 11 |
Reflection shell | Resolution: 3.599→3.728 Å / Num. unique obs: 596 / CC1/2: 0.525 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1U3C Resolution: 3.59936165826→30.6012670848 Å / SU ML: 0.455975310619 / Cross valid method: THROUGHOUT / σ(F): 1.33792184465 / Phase error: 26.6927274577 Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 57.7565723716 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3.59936165826→30.6012670848 Å
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Refine LS restraints |
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LS refinement shell |
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