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Yorodumi- EMDB-53844: Cryo-EM structure of Arabidopsis TIR-NLR WRR4A tetramer in comple... -
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Open data
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Basic information
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| Title | Cryo-EM structure of Arabidopsis TIR-NLR WRR4A tetramer in complex with weakly bound effector CCG28 (C2-symmetry) | |||||||||
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Keywords | TIR NLR / Resistosome / Oomycete / effector WRR4A / PLANT PROTEIN | |||||||||
| Function / homology | Function and homology informationdefense response to oomycetes / ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase / NAD+ nucleosidase activity, cyclic ADP-ribose generating / defense response to fungus / defense response / ADP binding / cellular response to UV / signal transduction / ATP binding / cytoplasm Similarity search - Function | |||||||||
| Biological species | ![]() Albugo candida (eukaryote) | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.5 Å | |||||||||
Authors | Zhao H / Lukoyanova N / Selvaraj M / Jones J | |||||||||
| Funding support | United Kingdom, 1 items
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Citation | Journal: Biorxiv / Year: 2026Title: Structural basis for the broad recognition specificity of an Arabidopsis immune receptor Authors: Zhao H / Szymansky CM / Lyu X / Huang J / Derbyshire P / Menke FLH / Webster MW / Kamoun S / Selvaraj M / Jones JDG | |||||||||
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Structure visualization
| Supplemental images |
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Downloads & links
-EMDB archive
| Map data | emd_53844.map.gz | 25.8 MB | EMDB map data format | |
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| Header (meta data) | emd-53844-v30.xml emd-53844.xml | 21.4 KB 21.4 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_53844_fsc.xml | 14.3 KB | Display | FSC data file |
| Images | emd_53844.png | 70 KB | ||
| Masks | emd_53844_msk_1.map | 244.1 MB | Mask map | |
| Filedesc metadata | emd-53844.cif.gz | 7.2 KB | ||
| Others | emd_53844_half_map_1.map.gz emd_53844_half_map_2.map.gz | 192.1 MB 192.2 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-53844 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-53844 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9r8wMC ![]() 9qlvC ![]() 9qt4C ![]() 9qu9C M: atomic model generated by this map C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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| Related items in Molecule of the Month |
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Map
| File | Download / File: emd_53844.map.gz / Format: CCP4 / Size: 244.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 0.828 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Mask #1
| File | emd_53844_msk_1.map | ||||||||||||
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-Half map: #2
| File | emd_53844_half_map_1.map | ||||||||||||
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-Half map: #1
| File | emd_53844_half_map_2.map | ||||||||||||
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| Density Histograms |
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Sample components
-Entire : WRR4A tetramer in complex with loosely bound effector CCG28
| Entire | Name: WRR4A tetramer in complex with loosely bound effector CCG28 |
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| Components |
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-Supramolecule #1: WRR4A tetramer in complex with loosely bound effector CCG28
| Supramolecule | Name: WRR4A tetramer in complex with loosely bound effector CCG28 type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2 |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 600 KDa |
-Macromolecule #1: Effector CCG28
| Macromolecule | Name: Effector CCG28 / type: protein_or_peptide / ID: 1 / Number of copies: 4 / Enantiomer: LEVO |
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| Source (natural) | Organism: Albugo candida (eukaryote) |
| Molecular weight | Theoretical: 61.221621 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: MYLSLLSCRI MVHQHWLLFS FLWLLTAANQ RGIITVEFNH KSDLSRCQSC LVDIAGLDRL SLTSISTNDL SIKIAKFQAS GQACSFISA KLDCRHQTKC GSVTVTILEH VESLASSSNL QIAVNEQLKP LCILTSVQTS FDCGLCLRMT SSSEGIQKLK L ITMDTKEY ...String: MYLSLLSCRI MVHQHWLLFS FLWLLTAANQ RGIITVEFNH KSDLSRCQSC LVDIAGLDRL SLTSISTNDL SIKIAKFQAS GQACSFISA KLDCRHQTKC GSVTVTILEH VESLASSSNL QIAVNEQLKP LCILTSVQTS FDCGLCLRMT SSSEGIQKLK L ITMDTKEY YLHVLHTHQR NIFEPCSLSG VCSGIQYEFD AEYCDHLVKK LFVPRPYSSE HVIFPSSVDY TGPQELASAV RA IHCTVKW ELQCIQFITS QKPRRNCLAC MSDVSSRMAL LVALSSIEYG YEGYREGDTQ YLFFVIVQAA FDFYLQCDET CGR ITFHSL DSCISLAIKT NNVSPSQGKI YYNMVQRDLK KKEAVQETML IPQTSSCMWV EHELGEREWC KVCLQHLSKI DAKI LSSID FLVLSEESLH TISGCISFGS ELGMKLCKKV TPIPDQFCHS FDMLPSSHGY DIMAPSLPKI KHLVSTGRPK TPDID CFTC LTSTLDILIT DLVRFWMVGF PEESTCYSTC GTLKMDDRQV LDISMIRLMS SNTIGSRFN |
-Macromolecule #2: Disease resistance protein ADR2
| Macromolecule | Name: Disease resistance protein ADR2 / type: protein_or_peptide / ID: 2 / Number of copies: 4 / Enantiomer: LEVO / EC number: ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 114.119039 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: MASSSSSPRN WRYNVFTSFH GPDVRIKFLS HLRQQFVYNG ITMFDDNGIE RSQIIAPALK KAIGESRVAI VLLSKNYASS SWCLDELLE ILKCKEYIGQ IVMTVFYEVD PSHVRKQTGD FGIAFKETCA HKTEEERSKW SQALTYVGNI AGEDFIHWKD E AKMIEKIA ...String: MASSSSSPRN WRYNVFTSFH GPDVRIKFLS HLRQQFVYNG ITMFDDNGIE RSQIIAPALK KAIGESRVAI VLLSKNYASS SWCLDELLE ILKCKEYIGQ IVMTVFYEVD PSHVRKQTGD FGIAFKETCA HKTEEERSKW SQALTYVGNI AGEDFIHWKD E AKMIEKIA RDVSTKINVT PCRDFDDMVG LERHLKEMVS LLDLDKEGVK MVGISGPAGI GKSTIAKALH SRHSSTFQHN CF VDNLWEN YKICTGEHGV KLRLHEQFVS KILKQNGLEL THLSVIKDRL QDKKVLIILD DVESLAQLET LADMTWFGPG SRV IVTTEN KEILQQHGIG DIYQVGYPSE SEALTIFCLS AFKQASPPDG FMDLADEVVR ICDKLPLALC VLGSSLLRKS QTDW EDELP RLRNCLDGIE SVLKVGFESL NEKDQALFLY ITVFFNYECA DHVTLMLAKS NLNVRLGLKN LANRYLIHID HDQKK RVVV HRLLRVMAIQ VCTKQKPWKS QILVDAEKIA YVLEEATGNR SIKGVSFDTA EIDELMISPK AFEKMCNLLF LKVYDA GWH TGKRKLDIPE DIKFPRTIRL FHWDAYSGKR LPSSFFAENL VEVNMQDSEL QKLWEGTQCL ANLKKIDLSR SSCLTEL PD LSNATNLEDL YVGSCTALVE LPSSIGNLHK LAHIMMYSCE SLEVIPSLIN LTSLTFLNMN KCSRLRRFPD IPTSIEDV Q VTGTTLEELP ASLTHCSGLQ TIKISGSVNL KIFYTELPVS VSHINISNSG IEWITEDCIK GLHNLHDLCL SGCKRLVSL PELPRSLKIL QADDCDSLES LNGHLNTPNA ELYFANCFKL DAEARRAIIQ QSFVSGWALL PGLEVPPEFG HRARGNSLII PYSASNRFK VCVVMSLNHH QPFELVPRNL LYRWTVIGDS VSSDEKTFHL SHMFNADSVN SKLQKPHLFI FHSCLPFIFH S CLPFIFDI SNIMLEFSSE YKDFDILECG VQILTDETDE RNIWGSLVF UniProtKB: Disease resistance protein ADR2 |
-Macromolecule #3: ADENOSINE-5'-DIPHOSPHATE
| Macromolecule | Name: ADENOSINE-5'-DIPHOSPHATE / type: ligand / ID: 3 / Number of copies: 4 / Formula: ADP |
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| Molecular weight | Theoretical: 427.201 Da |
| Chemical component information | ![]() ChemComp-ADP: |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Concentration | 0.3 mg/mL |
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| Buffer | pH: 7.5 / Details: 150mM NaCl, 150mM Tris HCl, |
| Grid | Model: C-flat-2/1 / Support film - Material: GRAPHENE OXIDE / Pretreatment - Type: GLOW DISCHARGE |
| Vitrification | Cryogen name: ETHANE / Chamber humidity: 95 % / Chamber temperature: 5 K / Instrument: FEI VITROBOT MARK IV |
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Electron microscopy
| Microscope | TFS KRIOS |
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| Image recording | Film or detector model: GATAN K3 BIOCONTINUUM (6k x 4k) / Average electron dose: 50.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | C2 aperture diameter: 50.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 27.0 µm / Nominal defocus min: 14.0 µm / Nominal magnification: 105000 |
| Sample stage | Specimen 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
-Atomic model buiding 1
| Initial model | Chain - Source name: AlphaFold / Chain - Initial model type: in silico model |
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| Software | Name: Coot |
| Refinement | Protocol: FLEXIBLE FIT / Overall B value: 50 |
| Output model | ![]() PDB-9r8w: |
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About Yorodumi



Keywords
Albugo candida (eukaryote)
Authors
United Kingdom, 1 items
Citation








Z (Sec.)
Y (Row.)
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FIELD EMISSION GUN

