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- EMDB-22380: Structure of the activated Roq1 resistosome directly recognizing ... -
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Open data
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Basic information
Entry | Database: EMDB / ID: EMD-22380 | |||||||||
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Title | Structure of the activated Roq1 resistosome directly recognizing the pathogen effector XopQ | |||||||||
![]() | Structure of the activated Roq1 resistosome directly recognizing the pathogen effector XopQ | |||||||||
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![]() | Resistosome / ![]() ![]() | |||||||||
Function / homology | ![]() NADP+ nucleosidase activity / ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase / NAD+ nucleotidase, cyclic ADP-ribose generating / ![]() ![]() ![]() Similarity search - Function | |||||||||
Biological species | ![]() ![]() ![]() ![]() ![]() | |||||||||
Method | ![]() ![]() | |||||||||
![]() | Martin R / Qi T | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Structure of the activated ROQ1 resistosome directly recognizing the pathogen effector XopQ. Authors: Raoul Martin / Tiancong Qi / Haibo Zhang / Furong Liu / Miles King / Claire Toth / Eva Nogales / Brian J Staskawicz / ![]() ![]() Abstract: Plants and animals detect pathogen infection using intracellular nucleotide-binding leucine-rich repeat receptors (NLRs) that directly or indirectly recognize pathogen effectors and activate an ...Plants and animals detect pathogen infection using intracellular nucleotide-binding leucine-rich repeat receptors (NLRs) that directly or indirectly recognize pathogen effectors and activate an immune response. How effector sensing triggers NLR activation remains poorly understood. Here we describe the 3.8-angstrom-resolution cryo-electron microscopy structure of the activated ROQ1 (recognition of XopQ 1), an NLR native to with a Toll-like interleukin-1 receptor (TIR) domain bound to the effector XopQ ( outer protein Q). ROQ1 directly binds to both the predicted active site and surface residues of XopQ while forming a tetrameric resistosome that brings together the TIR domains for downstream immune signaling. Our results suggest a mechanism for the direct recognition of effectors by NLRs leading to the oligomerization-dependent activation of a plant resistosome and signaling by the TIR domain. | |||||||||
History |
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Structure visualization
Movie |
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Structure viewer | EM map: ![]() ![]() ![]() |
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 387.6 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 17.6 KB 17.6 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 16.9 KB | Display | ![]() |
Images | ![]() | 80.1 KB | ||
Filedesc metadata | ![]() | 7 KB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 7jluMC ![]() 7jlvC ![]() 7jlxC M: atomic model generated by this map C: citing same article ( |
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Similar structure data |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
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Annotation | Structure of the activated Roq1 resistosome directly recognizing the pathogen effector XopQ | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 0.9386 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
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Sample components
-Entire : Roq1
Entire | Name: Roq1 |
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Components |
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-Supramolecule #1: Roq1
Supramolecule | Name: Roq1 / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2 |
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Source (natural) | Organism: ![]() ![]() ![]() |
Molecular weight | Theoretical: 49.819 KDa |
-Supramolecule #2: XopQ
Supramolecule | Name: XopQ / type: complex / ID: 2 / Parent: 1 / Macromolecule list: #2 |
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Source (natural) | Organism: ![]() ![]() |
-Macromolecule #1: Disease resistance protein Roq1
Macromolecule | Name: Disease resistance protein Roq1 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO / EC number: ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase |
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Source (natural) | Organism: ![]() ![]() ![]() |
Molecular weight | Theoretical: 153.367109 KDa |
Recombinant expression | Organism: ![]() ![]() ![]() |
Sequence | String: MLTSSSHHGR SYDVFLSFRG EDTRKTFVGH LFNALIEKGI HTFMDDKELK RGKSISSELM KAIGESRFAV VVFSKNYASS TWCLEELVK ILEIHEKFEL IVVPVFYDVD PSTVRKQNGE YAVCFTKFEA NLVDDRDKVL RWREALTKVA NISGHDLRNT Y NGDESKCI ...String: MLTSSSHHGR SYDVFLSFRG EDTRKTFVGH LFNALIEKGI HTFMDDKELK RGKSISSELM KAIGESRFAV VVFSKNYASS TWCLEELVK ILEIHEKFEL IVVPVFYDVD PSTVRKQNGE YAVCFTKFEA NLVDDRDKVL RWREALTKVA NISGHDLRNT Y NGDESKCI QQILKDIFDK FCFSISITNR DLVGIESQIK KLSSLLRMDL KGVRLVGIWG MGGVGKTTAA RALFNRYYQN FE SACFLED VKEYLQHHTL LYLQKTLLSK LLKVEFVDCT DTEEMCVILK RRLCSKKVLV VLDDVNHNDQ LDKLVGAEDW FGS GSRIVI TTRDMKLLKN HDVHETYEIK VLEKDEAIEL FNLHAFKRSS PEKEFKELLN LVVDYTGGLP LALKVLGSLL YKED LDVWI STIDRLKDNP EGEIMATLKI SFDGLRDYEK SIFLDIACFF RGYNQRDMTA LFHASGFHPV LGVKTLVEKS LIFIL EDKI QMHDLMQEMG RQIAVQESPM RRIYRPEDVK DACIGDMRKE AIEGLLLTEP EQFEEGELEY MYSAEALKKT RRLRIL VKE YYNRGFDEPV AYLPNSLLWL EWRNYSSNSF PSNFEPSKLV YLTMKGSSII ELWNGAKRLA FLTTLDLSYC HKLIQTP DF RMITNLERLI LSSCDALVEV HPSVGFLKNL ILLNMDHCIS LERLPAIIQS ECLEVLDLNY CFNLKMFPEV ERNMTHLK K LDLTSTGIRE LPASIEHLSS LENLQMHSCN QLVSLPSSIW RFRNLKISEC EKLGSLPEIH GNSNCTRELI LKLVSIKEL PTSIGNLTSL NFLEICNCKT ISSLSSSIWG LTSLTTLKLL DCRKLKNLPG IPNAINHLSG HGLQLLLTLE QPTIYERLDL LRIIDMSWC SCISSLPHNI WMLKFLRILC ISYCSRLEYL PENLGHLEHL EELLADGTGI LRLPSSVARL NKLEVLSFRK K FAIGPKVQ YSSSMLNLPD DVFGSLGSLG SVVKLNLSGN GFCNLPETMN QLFCLEYLDI TFCQRLEALP ELPPSIKELY VD EHLALRI MEDLVIKCKE LNLIAVTKIE YQNFYRWLDS IWSDVSELLE NSQKQQLDDM LQLIPFSYLS TAKREEVLKI VIH GTRIPE WFRWQDRSAT TMSVNLPEYW YTENFLGFAI CCSCCFYHSA RSYDVEFEGS MHHYNYDSSY WKEYEEPSYD FYER DSIEI TAKLTPRHKG MRTEELKKVC SFSMNVLRRA TAVPNMCFAF FPFNSLCHIS NLQANNPNDY GIFETCLSPG DIRHR GKQW GFNLVYKDET GGSVTHEMLI NRDYKDHDGD YKDHDIDYKD DDDK UniProtKB: ![]() |
-Macromolecule #2: XopQ
Macromolecule | Name: XopQ / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 51.341492 KDa |
Recombinant expression | Organism: ![]() ![]() ![]() |
Sequence | String: MASWSHPQFE KGAMQPTAIR STVGLPGADM TADLRDPAPV AVPAHSAADA AAPPPGALQT IVGRPPRPDG PRHRRAQSLP ARLTPAQRG MLAELGVADT SVLTPTETAV LRELRLHRPP LPLDTLLFTD PNKDPDDVVT YTIAKQLQAE GFLRLTDVVV T LGDADMRS ...String: MASWSHPQFE KGAMQPTAIR STVGLPGADM TADLRDPAPV AVPAHSAADA AAPPPGALQT IVGRPPRPDG PRHRRAQSLP ARLTPAQRG MLAELGVADT SVLTPTETAV LRELRLHRPP LPLDTLLFTD PNKDPDDVVT YTIAKQLQAE GFLRLTDVVV T LGDADMRS QRAQLAKGVF DRLALPEVRV ARGQDYPMTS TQAREHSKFL AEGAALRAAP DAVHTDGVRA MRERLATSPH KL GMVVIAG MTDASALLAE AGDLVREKLA SITIMGGIDP ARDADGLVQP DTRAYNNATD IHAARALYRR AQQLGIPLRI LSK EAAYRA AVPPAFYEGI ARNGHPVGEY LRDVQKNALK GLWEGIQANL IPGLDTAWFF RTFVAAQPQD PAAADQQGAM SFDA IWPQV TKLNLYDPLT LLAALPGAAR LLFQPTPMHR EGASPVEHVG HAEVVRPEKA RLLLSALAKA ALAQQDEGQR GR UniProtKB: XopQ |
-Macromolecule #3: CALCIUM ION
Macromolecule | Name: CALCIUM ION / type: ligand / ID: 3 / Number of copies: 1 / Formula: CA |
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Molecular weight | Theoretical: 40.078 Da |
-Experimental details
-Structure determination
Method | ![]() |
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Aggregation state | particle |
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Sample preparation
Buffer | pH: 7.5 Component:
Details: Kept at 4 degrees Celsius. | ||||||||||||||
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Grid | Model: Quantifoil R2/2 / Material: COPPER / Mesh: 400 / Support film - Material: CARBON / Support film - topology: CONTINUOUS / Pretreatment - Type: PLASMA CLEANING | ||||||||||||||
Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277.15 K / Instrument: FEI VITROBOT MARK IV / Details: 90 min incubation. 10 sec blot. Blot Force 10.. | ||||||||||||||
Details | Sample was monodisperse. |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Calibrated magnification: 80879 / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD![]() |
Specialist optics | Energy filter - Name: GIF Bioquantum |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
Image recording | Film or detector model: GATAN K3 (6k x 4k) / Number grids imaged: 1 / Number real images: 11134 / Average electron dose: 50.0 e/Å2 Details: Images were collected as dose-fractionated movie frames. |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
-Atomic model buiding 1
Refinement | Space: REAL |
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Output model | ![]() PDB-7jlu: |