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- EMDB-62397: Strigolactone-induced ASK1-MAX2-HTL7-SMAX1 complex (Class 1) with... -

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Basic information

Entry
Database: EMDB / ID: EMD-62397
TitleStrigolactone-induced ASK1-MAX2-HTL7-SMAX1 complex (Class 1) with covalently bound D-ring
Map dataUnsharpened map of ASK1-MAX2-HTL7-SMAX1 Class 1
Sample
  • Complex: Strigolactone signalling complex of ASK1-MAX2-HTL-SMAX1 induced by GR24
    • Complex: ASK1-SMAX1
      • Protein or peptide: Protein SUPPRESSOR OF MAX2 1
      • Protein or peptide: SKP1-like protein 1A
    • Complex: MAX2-HTL7
      • Protein or peptide: Hyposensitive to light 7
      • Protein or peptide: F-box protein
  • Ligand: (3E,3aR,8bS)-3-({[(2R)-4-methyl-5-oxo-2,5-dihydrofuran-2-yl]oxy}methylidene)-3,3a,4,8b-tetrahydro-2H-indeno[1,2-b]furan-2-one
KeywordsStrigolactone / SCF / Ubiquitination / SIGNALING PROTEIN
Function / homology
Function and homology information


response to strigolactone / response to karrikin / seedling development / phragmoplast / seed germination / jasmonic acid mediated signaling pathway / ethylene-activated signaling pathway / response to jasmonic acid / response to auxin / auxin-activated signaling pathway ...response to strigolactone / response to karrikin / seedling development / phragmoplast / seed germination / jasmonic acid mediated signaling pathway / ethylene-activated signaling pathway / response to jasmonic acid / response to auxin / auxin-activated signaling pathway / negative regulation of DNA recombination / SCF ubiquitin ligase complex / SCF-dependent proteasomal ubiquitin-dependent protein catabolic process / chromosome segregation / microtubule cytoskeleton organization / spindle / ubiquitin-dependent protein catabolic process / protein ubiquitination / ATP hydrolysis activity / mitochondrion / ATP binding / metal ion binding / nucleus / cytosol
Similarity search - Function
SMAX1 nucleotide binding domain / : / COI1, F-box / F-box / Leucine-rich repeat, cysteine-containing subtype / Leucine-rich repeat - CC (cysteine-containing) subfamily / SKP1 component, dimerisation / S-phase kinase-associated protein 1 / SKP1-like, dimerisation domain superfamily / Skp1 family, dimerisation domain ...SMAX1 nucleotide binding domain / : / COI1, F-box / F-box / Leucine-rich repeat, cysteine-containing subtype / Leucine-rich repeat - CC (cysteine-containing) subfamily / SKP1 component, dimerisation / S-phase kinase-associated protein 1 / SKP1-like, dimerisation domain superfamily / Skp1 family, dimerisation domain / Alpha/beta hydrolase family / Clp, repeat (R) domain / Clp repeat (R) domain profile. / Clp, N-terminal domain superfamily / AAA domain (Cdc48 subfamily) / S-phase kinase-associated protein 1-like / SKP1 component, POZ domain / Skp1 family, tetramerisation domain / Found in Skp1 protein family / Alpha/beta hydrolase fold-1 / SKP1/BTB/POZ domain superfamily / Leucine-rich repeat domain superfamily / ATPase, AAA-type, core / Alpha/Beta hydrolase fold / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
Hyposensitive to light 7 / SKP1-like protein 1A / Protein SUPPRESSOR OF MAX2 1 / F-box protein
Similarity search - Component
Biological speciesArabidopsis thaliana (thale cress) / Striga hermonthica (purple witchweed)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.8 Å
AuthorsVancea AI / Huntington B / Savva CG / Arold ST
Funding support Saudi Arabia, 1 items
OrganizationGrant numberCountry
Other privateURF/1/4039-01-01 & URF/1/4080-01-01 Saudi Arabia
CitationJournal: To Be Published
Title: Mechanism of cooperative strigolactone perception by the MAX2 ubiquitin ligase-receptor-substrate complex
Authors: Vancea AI / Huntington B / Steinchen W / Savva CG / Hameed UFS / Arold ST
History
DepositionNov 14, 2024-
Header (metadata) releaseSep 17, 2025-
Map releaseSep 17, 2025-
UpdateSep 17, 2025-
Current statusSep 17, 2025Processing site: PDBj / Status: Released

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Structure visualization

Supplemental images

Downloads & links

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Map

FileDownload / File: emd_62397.map.gz / Format: CCP4 / Size: 178 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationUnsharpened map of ASK1-MAX2-HTL7-SMAX1 Class 1
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.73 Å/pix.
x 360 pix.
= 262.8 Å
0.73 Å/pix.
x 360 pix.
= 262.8 Å
0.73 Å/pix.
x 360 pix.
= 262.8 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.73 Å
Density
Contour LevelBy AUTHOR: 0.00374
Minimum - Maximum-0.008405523 - 0.023102218
Average (Standard dev.)0.000024316561 (±0.0006325923)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions360360360
Spacing360360360
CellA=B=C: 262.80002 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_62397_msk_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

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Additional map: sharpened map of ASK1-MAX2-HTL7-SMAX1 Class 1

Fileemd_62397_additional_1.map
Annotationsharpened map of ASK1-MAX2-HTL7-SMAX1 Class 1
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

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Additional map: EMReady post-processed map from unsharpened primary map

Fileemd_62397_additional_2.map
AnnotationEMReady post-processed map from unsharpened primary map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

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Half map: #2

Fileemd_62397_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

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Half map: #1

Fileemd_62397_half_map_2.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

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Sample components

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Entire : Strigolactone signalling complex of ASK1-MAX2-HTL-SMAX1 induced b...

EntireName: Strigolactone signalling complex of ASK1-MAX2-HTL-SMAX1 induced by GR24
Components
  • Complex: Strigolactone signalling complex of ASK1-MAX2-HTL-SMAX1 induced by GR24
    • Complex: ASK1-SMAX1
      • Protein or peptide: Protein SUPPRESSOR OF MAX2 1
      • Protein or peptide: SKP1-like protein 1A
    • Complex: MAX2-HTL7
      • Protein or peptide: Hyposensitive to light 7
      • Protein or peptide: F-box protein
  • Ligand: (3E,3aR,8bS)-3-({[(2R)-4-methyl-5-oxo-2,5-dihydrofuran-2-yl]oxy}methylidene)-3,3a,4,8b-tetrahydro-2H-indeno[1,2-b]furan-2-one

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Supramolecule #1: Strigolactone signalling complex of ASK1-MAX2-HTL-SMAX1 induced b...

SupramoleculeName: Strigolactone signalling complex of ASK1-MAX2-HTL-SMAX1 induced by GR24
type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#4

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Supramolecule #2: ASK1-SMAX1

SupramoleculeName: ASK1-SMAX1 / type: complex / ID: 2 / Parent: 1 / Macromolecule list: #1-#2
Source (natural)Organism: Arabidopsis thaliana (thale cress)

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Supramolecule #3: MAX2-HTL7

SupramoleculeName: MAX2-HTL7 / type: complex / ID: 3 / Parent: 1 / Macromolecule list: #3-#4
Source (natural)Organism: Striga hermonthica (purple witchweed)

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Macromolecule #1: Protein SUPPRESSOR OF MAX2 1

MacromoleculeName: Protein SUPPRESSOR OF MAX2 1 / type: protein_or_peptide / ID: 1 / Details: N-terminal 7xHis tag and C-terminal Strep tag / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Arabidopsis thaliana (thale cress)
Molecular weightTheoretical: 113.453078 KDa
Recombinant expressionOrganism: Escherichia coli BL21(DE3) (bacteria)
SequenceString: MKHHHHHHHG AAGTSLYKKA GENLYFQGSM RAGLSTIQQT LTPEAATVLN QSIAEAARRN HGQTTPLHVA ATLLASPAGF LRRACIRSH PNSSHPLQCR ALELCFSVAL ERLPTATTTP GNDPPISNAL MAALKRAQAH QRRGCPEQQQ QPLLAVKVEL E QLIISILD ...String:
MKHHHHHHHG AAGTSLYKKA GENLYFQGSM RAGLSTIQQT LTPEAATVLN QSIAEAARRN HGQTTPLHVA ATLLASPAGF LRRACIRSH PNSSHPLQCR ALELCFSVAL ERLPTATTTP GNDPPISNAL MAALKRAQAH QRRGCPEQQQ QPLLAVKVEL E QLIISILD DPSVSRVMRE ASFSSPAVKA TIEQSLNNSV TPTPIPSVSS VGLNFRPGGG GPMTRNSYLN PRLQQNASSV QS GVSKNDD VERVMDILGR AKKKNPVLVG DSEPGRVIRE ILKKIEVGEV GNLAVKNSKV VSLEEISSDK ALRIKELDGL LQT RLKNSD PIGGGGVILD LGDLKWLVEQ PSSTQPPATV AVEIGRTAVV ELRRLLEKFE GRLWFIGTAT CETYLRCQVY HPSV ETDWD LQAVSVAAKA PASGVFPRLA NNLESFTPLK SFVPANRTLK CCPQCLQSYE RELAEIDSVS SPEVKSEVAQ PKQLP QWLL KAKPVDRLPQ AKIEEVQKKW NDACVRLHPS FHNKNERIVP IPVPITLTTS PYSPNMLLRQ PLQPKLQPNR ELRERV HLK PMSPLVAEQA KKKSPPGSPV QTDLVLGRAE DSEKAGDVQV RDFLGCISSE SVQNNNNISV LQKENLGNSL DIDLFKK LL KGMTEKVWWQ NDAAAAVAAT VSQCKLGNGK RRGVLSKGDV WLLFSGPDRV GKRKMVSALS SLVYGTNPIM IQLGSRQD A GDGNSSFRGK TALDKIAETV KRSPFSVILL EDIDEADMLV RGSIKQAMDR GRIRDSHGRE ISLGNVIFVM TASWHFAGT KTSFLDNEAK LRDLASESWR LRLCMREKFG KRRASWLCSD EERLTKPKKE HGSGLSFDLN QAADTDDGSH NTSDLTTDND QDEQGFSGK LSLQCVPFAF HDMVSRVDDA VAFRAVDFAA VRRRITETLS ERFETIIGES LSVEVEEEAL QRILSGVWLG Q TELEEWIE KAIVPVLSQL KARVSSSGTY GDCTVARLEL DEDSGERNAG DLLPTTITLA VGSGSWSHPQ FEK

UniProtKB: Protein SUPPRESSOR OF MAX2 1

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Macromolecule #2: SKP1-like protein 1A

MacromoleculeName: SKP1-like protein 1A / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Arabidopsis thaliana (thale cress)
Molecular weightTheoretical: 17.876043 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString:
MSAKKIVLKS SDGESFEVEE AVALESQTIA HMVEDDCVDN GVPLPNVTSK ILAKVIEYCK RHVEAAASKA EAVEGAATSD DDLKAWDAD FMKIDQATLF ELILAANYLN IKNLLDLTCQ TVADMIKGKT PEEIRTTFNI KNDFTPEEEE EVRRENQWAF E

UniProtKB: SKP1-like protein 1A

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Macromolecule #3: Hyposensitive to light 7

MacromoleculeName: Hyposensitive to light 7 / type: protein_or_peptide / ID: 3 / Details: N-terminal 7xHis tag / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Striga hermonthica (purple witchweed)
Molecular weightTheoretical: 33.472352 KDa
Recombinant expressionOrganism: Escherichia coli BL21(DE3) (bacteria)
SequenceString: MKHHHHHHHG AAGTSLYKKA GENLYFQGSM SSIGLAHNVT ILGSGETTVV LGHGYGTDQS VWKLLVPYLV DDYKVLLYDH MGAGTTNPD YFDFDRYSSL EGYSYDLIAI LEEFQVSKCI YVGHSMSSMA AAVASIFRPD LFHKLVMISP TPRLINTEEY Y GGFEQKVM ...String:
MKHHHHHHHG AAGTSLYKKA GENLYFQGSM SSIGLAHNVT ILGSGETTVV LGHGYGTDQS VWKLLVPYLV DDYKVLLYDH MGAGTTNPD YFDFDRYSSL EGYSYDLIAI LEEFQVSKCI YVGHSMSSMA AAVASIFRPD LFHKLVMISP TPRLINTEEY Y GGFEQKVM DETLRSLDEN FKSLSLGTAP LLLACDLESA AMQEYCRTLF NMRPDIACCI TRMICGLDLR PYLGHVTVPC HI IQSSNDI MVPVAVGEYL RKNLGGPSVV EVMPTEGHLP HLSMPEVTIP VVLRHIRQDI TDH

UniProtKB: Hyposensitive to light 7

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Macromolecule #4: F-box protein

MacromoleculeName: F-box protein / type: protein_or_peptide / ID: 4 / Details: N-terminal 9xHis and Strep-tag / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Striga hermonthica (purple witchweed)
Molecular weightTheoretical: 85.626188 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString: MHHHHHHHHH SSGWSHPQFE KGGGSGGGSL EVLFQGPLTP KTNYIPFPSP IHQTPFQTDL APMAAAAAAA TTALNDLPDV ILSNIMAGV SDVRSRNSAS LVCHKWYLLE RATRSALTLR GNIRDLFMLP TCFQSTSHLD LSLISPWGHP LTSAADPDSA L IGHLLRHA ...String:
MHHHHHHHHH SSGWSHPQFE KGGGSGGGSL EVLFQGPLTP KTNYIPFPSP IHQTPFQTDL APMAAAAAAA TTALNDLPDV ILSNIMAGV SDVRSRNSAS LVCHKWYLLE RATRSALTLR GNIRDLFMLP TCFQSTSHLD LSLISPWGHP LTSAADPDSA L IGHLLRHA FPSVTSLAIY ARDPSTIHIV VPQWPDLERL KLVRWHQRPQ TDAAGDELKL LISECGTLKS LDLSSFYCWT DD VPAALGS CPTFAANLKS LNLLNSSFSE GFKSDEIKAI TKACPNLREF RASCMFDPRY IGHAGDEALV SISVNCPKLE ILH LADTNA LSSARSDFDP DEREGLGQEE AKINAATLIE VFSGLPLLEE LALDLCNNVR DSGPALEVLN SKCPKLKSVK LGQF HGISL PVESKLDGIA LCQGLESLSI RNVDDLTDMG LIAIGRGCYR LAKFEVYGCK KITVRGMRTM ASLLRKTLVD VKIAA CKKL GAVQSLKALE PIQDRVERLH IDCDWDCPDE EEPSDYFDSA AEYNECDDEM YSVRKRARYT YDLNSSSSGL DVNVEG YDE DKTWARLRYV SLWIFVGQLL TPLVAAGLND CPELEEISIK VEGDCRVLSR PTVREFGLTT LLNYPKLSRM HLDCGDI NG YAHTAPSGQM DLSLWERFYL IGVGHLGLTE LNYWPPQDRD VNQRSLSLPA AGLLQECNRL RKLFIHGTAH EHFMMFFL R IEGLRDVQLR ADYYPAPEND MSTEMRADSC SRFEVALNRR QISDSSGSSG

UniProtKB: F-box protein

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Macromolecule #5: (3E,3aR,8bS)-3-({[(2R)-4-methyl-5-oxo-2,5-dihydrofuran-2-yl]oxy}m...

MacromoleculeName: (3E,3aR,8bS)-3-({[(2R)-4-methyl-5-oxo-2,5-dihydrofuran-2-yl]oxy}methylidene)-3,3a,4,8b-tetrahydro-2H-indeno[1,2-b]furan-2-one
type: ligand / ID: 5 / Number of copies: 1 / Formula: GR2
Molecular weightTheoretical: 298.29 Da
Chemical component information

ChemComp-GR2:
(3E,3aR,8bS)-3-({[(2R)-4-methyl-5-oxo-2,5-dihydrofuran-2-yl]oxy}methylidene)-3,3a,4,8b-tetrahydro-2H-indeno[1,2-b]furan-2-one

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

Concentration0.35 mg/mL
BufferpH: 7.5
Component:
ConcentrationFormulaName
20.0 mMC8H18N2O4SHEPES
200.0 mMNaClsodium chloride
0.5 mMC9H15O6PTCEP
GridModel: UltrAuFoil R1.2/1.3 / Material: GOLD / Mesh: 300 / Support film - Material: GOLD / Support film - topology: HOLEY / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 30 sec. / Pretreatment - Atmosphere: AIR
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV

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Electron microscopy

MicroscopeTFS KRIOS
TemperatureMin: 80.0 K / Max: 90.0 K
Specialist opticsEnergy filter - Name: TFS Selectris X / Energy filter - Slit width: 10 eV
Image recordingFilm or detector model: TFS FALCON 4i (4k x 4k) / Number grids imaged: 1 / Number real images: 20175 / Average exposure time: 3.0 sec. / Average electron dose: 44.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsC2 aperture diameter: 50.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 2.7 µm / Nominal defocus min: 1.5 µm / Nominal magnification: 165000
Sample stageSpecimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: INSILICO MODEL
Final reconstructionApplied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 2.8 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 60356
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
FSC plot (resolution estimation)

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Atomic model buiding 1

Initial model
ChainPDB ID
source_name: AlphaFold, initial_model_type: in silico model
source_name: SwissModel, initial_model_type: in silico model
RefinementSpace: REAL / Protocol: FLEXIBLE FIT
Output model

PDB-9kkx:
Strigolactone-induced ASK1-MAX2-HTL7-SMAX1 complex (Class 1) with covalently bound D-ring

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