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- PDB-6m79: Cryo-EM structure of Arabidopsis CRY under blue light-mediated ac... -

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Basic information

Entry
Database: PDB / ID: 6m79
TitleCryo-EM structure of Arabidopsis CRY under blue light-mediated activation
ComponentsCryptochrome-2
KeywordsTRANSCRIPTION / blue-light activated / Arabidopsis thaliana / CRY2 tetramer
Function / homology
Function and homology information


flavin adenine dinucleotide metabolic process / regulation of meristem growth / long-day photoperiodism, flowering / response to absence of light / response to strigolactone / regulation of leaf morphogenesis / circadian regulation of calcium ion oscillation / response to low fluence blue light stimulus by blue low-fluence system / regulation of flower development / positive regulation of flower development ...flavin adenine dinucleotide metabolic process / regulation of meristem growth / long-day photoperiodism, flowering / response to absence of light / response to strigolactone / regulation of leaf morphogenesis / circadian regulation of calcium ion oscillation / response to low fluence blue light stimulus by blue low-fluence system / regulation of flower development / positive regulation of flower development / regulation of photoperiodism, flowering / blue light signaling pathway / phototropism / stomatal movement / blue light photoreceptor activity / response to blue light / response to water deprivation / plant-type vacuole / response to light stimulus / FAD binding / circadian rhythm / regulation of circadian rhythm / positive regulation of reactive oxygen species metabolic process / chromatin organization / defense response to virus / nuclear body / chromatin remodeling / protein homodimerization activity / ATP binding / metal ion binding / identical protein binding / nucleus / cytoplasm
Similarity search - Function
Cryptochrome, plant / DNA photolyases class 1 signature 2. / Cryptochrome/DNA photolyase class 1, conserved site, C-terminal / DNA photolyases class 1 signature 1. / Cryptochrome/DNA photolyase class 1 / Cryptochrome/DNA photolyase, FAD-binding domain / FAD binding domain of DNA photolyase / DNA photolyase, N-terminal / Cryptochrome/photolyase, N-terminal domain superfamily / DNA photolyase ...Cryptochrome, plant / DNA photolyases class 1 signature 2. / Cryptochrome/DNA photolyase class 1, conserved site, C-terminal / DNA photolyases class 1 signature 1. / Cryptochrome/DNA photolyase class 1 / Cryptochrome/DNA photolyase, FAD-binding domain / FAD binding domain of DNA photolyase / 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 / Rossmann-like alpha/beta/alpha sandwich fold
Similarity search - Domain/homology
ADENOSINE MONOPHOSPHATE / FLAVIN-ADENINE DINUCLEOTIDE / Cryptochrome-2
Similarity search - Component
Biological speciesArabidopsis thaliana (thale cress)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.1 Å
AuthorsMa, L. / Guan, Z.Y. / Yin, P.
CitationJournal: Nat Plants / Year: 2020
Title: Structural insights into the photoactivation of Arabidopsis CRY2.
Authors: Ling Ma / Zeyuan Guan / Qiang Wang / Xuhui Yan / Jing Wang / Zhizheng Wang / Jianbo Cao / Delin Zhang / Xin Gong / Ping Yin /
Abstract: The blue-light receptor cryptochrome (CRY) in plants undergoes oligomerization to transduce blue-light signals after irradiation, but the corresponding molecular mechanism remains poorly understood. ...The blue-light receptor cryptochrome (CRY) in plants undergoes oligomerization to transduce blue-light signals after irradiation, but the corresponding molecular mechanism remains poorly understood. Here, we report the cryogenic electron microscopy structure of a blue-light-activated CRY2 tetramer at a resolution of 3.1 Å, which shows how the CRY2 tetramer assembles. Our study provides insights into blue-light-mediated activation of CRY2 and a theoretical basis for developing regulators of CRYs for optogenetic manipulation.
History
DepositionMar 18, 2020Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Oct 14, 2020Provider: repository / Type: Initial release
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Structure visualization

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Assembly

Deposited unit
A: Cryptochrome-2
B: Cryptochrome-2
C: Cryptochrome-2
D: Cryptochrome-2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)282,85112
Polymers278,3204
Non-polymers4,5318
Water00
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_5551
Buried area18680 Å2
ΔGint-79 kcal/mol
Surface area82580 Å2

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Components

#1: Protein
Cryptochrome-2 / Atcry2 / Blue light photoreceptor / Protein PHR homolog 1 / AtPHH1 / Protein SUPPRESSOR OF elf3 20


Mass: 69579.930 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Arabidopsis thaliana (thale cress) / Gene: CRY2, PHH1, SEL20, At1g04400, F19P19.14 / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: Q96524
#2: Chemical
ChemComp-AMP / ADENOSINE MONOPHOSPHATE


Mass: 347.221 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C10H14N5O7P / Feature type: SUBJECT OF INVESTIGATION / Comment: AMP*YM
#3: Chemical
ChemComp-FAD / FLAVIN-ADENINE DINUCLEOTIDE


Mass: 785.550 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C27H33N9O15P2 / Feature type: SUBJECT OF INVESTIGATION / Comment: FAD*YM
Has ligand of interestY
Has protein modificationN
Sequence detailsThese conflicts are derived from GenBank AAB04996.

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

ComponentName: blue-light activated Arabidopsis thaliana CRY2 tetramer
Type: COMPLEX / Entity ID: #1 / Source: RECOMBINANT
Source (natural)Organism: Arabidopsis thaliana (thale cress)
Source (recombinant)Organism: Spodoptera frugiperda (fall armyworm)
Buffer solutionpH: 8
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
VitrificationCryogen name: ETHANE

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: FEI TITAN KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: SPOT SCAN
Electron lensMode: BRIGHT FIELD
Image recordingElectron dose: 50 e/Å2 / Detector mode: SUPER-RESOLUTION / Film or detector model: GATAN K2 SUMMIT (4k x 4k)

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Processing

Software
NameVersionClassification
phenix.real_space_refine1.18.2_3874refinement
PHENIX1.18.2_3874refinement
EM software
IDNameVersionCategory
4Gctfv1.18CTF correction
7Coot0.8.9.1model fitting
9RELION3.0-beta-2initial Euler assignment
10RELION3.0-beta-2final Euler assignment
11RELION3.0-beta-2classification
12RELION3.0-beta-23D reconstruction
13PHENIX1.16model refinement
CTF correctionType: NONE
SymmetryPoint symmetry: C2 (2 fold cyclic)
3D reconstructionResolution: 3.1 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 209604 / Symmetry type: POINT
RefinementCross valid method: NONE
Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
Displacement parametersBiso mean: 9.98 Å2
Refine LS restraints
Refine-IDTypeDev idealNumber
ELECTRON MICROSCOPYf_bond_d0.007315804
ELECTRON MICROSCOPYf_angle_d0.702621554
ELECTRON MICROSCOPYf_chiral_restr0.04762266
ELECTRON MICROSCOPYf_plane_restr0.00442672
ELECTRON MICROSCOPYf_dihedral_angle_d20.41135678

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