+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-13790 | |||||||||
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Title | Structure of the mouse CPLANE-RSG1 complex | |||||||||
Map data | Full Map | |||||||||
Sample |
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Keywords | ciliogenesis / ciliopathies / longin / lipid binding / PROTEIN TRANSPORT | |||||||||
Function / homology | Function and homology information axonemal basal plate / respiratory system development / tongue morphogenesis / auditory receptor cell morphogenesis / regulation of embryonic cell shape / regulation of vesicle fusion / septin cytoskeleton organization / digestive system development / regulation of ruffle assembly / protein localization => GO:0008104 ...axonemal basal plate / respiratory system development / tongue morphogenesis / auditory receptor cell morphogenesis / regulation of embryonic cell shape / regulation of vesicle fusion / septin cytoskeleton organization / digestive system development / regulation of ruffle assembly / protein localization => GO:0008104 / regulation of fibroblast migration / podocyte cell migration / establishment of planar polarity / spinal cord dorsal/ventral patterning / motile cilium assembly / circulatory system development / cilium organization / Hedgehog 'off' state / negative regulation of cell division / regulation of exocytosis / positive regulation of cilium assembly / non-motile cilium assembly / regulation of smoothened signaling pathway / camera-type eye development / positive regulation of smoothened signaling pathway / motile cilium / regulation of establishment of cell polarity / limb development / neural tube development / regulation of focal adhesion assembly / embryonic digit morphogenesis / hair follicle morphogenesis / smoothened signaling pathway / roof of mouth development / exocytosis / axoneme / cilium assembly / regulation of ossification / negative regulation of keratinocyte proliferation / embryonic organ development / keratinocyte differentiation / vesicle-mediated transport / ciliary basal body / negative regulation of cell migration / kidney development / neural tube closure / establishment of protein localization / cilium / regulation of protein localization / protein transport / nervous system development / cytoskeleton / GTPase activity / GTP binding / cell surface / plasma membrane / cytoplasm Similarity search - Function | |||||||||
Biological species | Mus musculus (house mouse) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.35 Å | |||||||||
Authors | Langousis G / Cavadini S | |||||||||
Funding support | 2 items
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Citation | Journal: Sci Adv / Year: 2022 Title: Structure of the ciliogenesis-associated CPLANE complex. Authors: Gerasimos Langousis / Simone Cavadini / Niels Boegholm / Esben Lorentzen / Georg Kempf / Patrick Matthias / Abstract: Dysfunctional cilia cause pleiotropic human diseases termed ciliopathies. These hereditary maladies are often caused by defects in cilia assembly, a complex event that is regulated by the ...Dysfunctional cilia cause pleiotropic human diseases termed ciliopathies. These hereditary maladies are often caused by defects in cilia assembly, a complex event that is regulated by the ciliogenesis and planar polarity effector (CPLANE) proteins Wdpcp, Inturned, and Fuzzy. CPLANE proteins are essential for building the cilium and are mutated in multiple ciliopathies, yet their structure and molecular functions remain elusive. Here, we show that mammalian CPLANE proteins comprise a bona fide complex and report the near-atomic resolution structures of the human Wdpcp-Inturned-Fuzzy complex and of the mouse Wdpcp-Inturned-Fuzzy complex bound to the small guanosine triphosphatase Rsg1. Notably, the crescent-shaped CPLANE complex binds phospholipids such as phosphatidylinositol 3-phosphate via multiple modules and a CPLANE ciliopathy mutant exhibits aberrant lipid binding. Our study provides critical structural and functional insights into an enigmatic ciliogenesis-associated complex as well as unexpected molecular rationales for ciliopathies. | |||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_13790.map.gz | 50 MB | EMDB map data format | |
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Header (meta data) | emd-13790-v30.xml emd-13790.xml | 20.7 KB 20.7 KB | Display Display | EMDB header |
Images | emd_13790.png | 90.8 KB | ||
Filedesc metadata | emd-13790.cif.gz | 6.9 KB | ||
Others | emd_13790_additional_1.map.gz emd_13790_half_map_1.map.gz emd_13790_half_map_2.map.gz | 51 MB 83.4 MB 83.4 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-13790 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-13790 | HTTPS FTP |
-Validation report
Summary document | emd_13790_validation.pdf.gz | 1.1 MB | Display | EMDB validaton report |
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Full document | emd_13790_full_validation.pdf.gz | 1.1 MB | Display | |
Data in XML | emd_13790_validation.xml.gz | 13.3 KB | Display | |
Data in CIF | emd_13790_validation.cif.gz | 15.7 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-13790 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-13790 | HTTPS FTP |
-Related structure data
Related structure data | 7q3eMC 7q3dC M: atomic model generated by this map C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Related items in Molecule of the Month |
-Map
File | Download / File: emd_13790.map.gz / Format: CCP4 / Size: 103 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||
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Annotation | Full Map | ||||||||||||||||||||
Voxel size | X=Y=Z: 0.86 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Additional map: Sharpened with Locscale
File | emd_13790_additional_1.map | ||||||||||||
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Annotation | Sharpened with Locscale | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: Half map A
File | emd_13790_half_map_1.map | ||||||||||||
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Annotation | Half map A | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: Half map B
File | emd_13790_half_map_2.map | ||||||||||||
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Annotation | Half map B | ||||||||||||
Projections & Slices |
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Density Histograms |
-Sample components
-Entire : CPLANE complex
Entire | Name: CPLANE complex |
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Components |
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-Supramolecule #1: CPLANE complex
Supramolecule | Name: CPLANE complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#4 |
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Source (natural) | Organism: Mus musculus (house mouse) |
-Macromolecule #1: WD repeat-containing and planar cell polarity effector protein fr...
Macromolecule | Name: WD repeat-containing and planar cell polarity effector protein fritz homolog type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: Mus musculus (house mouse) |
Molecular weight | Theoretical: 86.286477 KDa |
Recombinant expression | Organism: Spodoptera frugiperda (fall armyworm) |
Sequence | String: MDSAWSHPQF EKGGGSGGGS GGSAWSHPQF EKSAVDLEVL FQGPGSFCLT ELHLWSLKST LHIADRDIGV YQYYDKKDPS VSATEHGNL EEKQRLAESR DYPWTLKNRR PEKLRDSLKE LEELMQSSPC VLSKWKSKYI CQLLFGSGVL VSLSLSGPQL E KVVIDRSL ...String: MDSAWSHPQF EKGGGSGGGS GGSAWSHPQF EKSAVDLEVL FQGPGSFCLT ELHLWSLKST LHIADRDIGV YQYYDKKDPS VSATEHGNL EEKQRLAESR DYPWTLKNRR PEKLRDSLKE LEELMQSSPC VLSKWKSKYI CQLLFGSGVL VSLSLSGPQL E KVVIDRSL VGKLISDTIS DALLTDSFII LSFLAQNKLC FIQFTKKMDS LDGNKRLEKL SALDLKISYY DIPGPANRTI DR HLAVNST QDLVVCWWPL VSDDVWPWTP VSSEKDRANM LLLGFTQGGL EVLSFVRTEW SPLDVHFGTK QPYQVFTVEC SVS VDKEPM ADSCIYESVR NKLHCVSVTR IPLRSKAISC CRNSTEDKLI VGCEDSSVIL YEAHRGVTLL AQAELRPSLI SCHP SGAIL LVGSNQGELQ IFDIALSPIN IQLLAEDYSP KETLQFKKFF DVSSSLVQMQ WMAPPVVFQK PKRGEICDLL FLRFN KGPL GVLLFKLGIL TRGQLGLVDL ILQYIHYSEV YEAISILRSM DWDTLGQQCL IGMGTIVNHL LRQRLTPERE AQLEAS LGT FYAPTRPLLD TTILEYREPV SKYARRLFHH LLRYKRFEKA FLLAVDIGAR DLFMDIHYLA LDMGELALAE VARRRAH DI DVESVSSGVE LLGPLDRRDM LNEGFASSAL MPEGENKFPG LLPSIGSTHM QTLQQKIPNG PSSRWAIERR TEEEEEEE E EEEEELCTDS SGATTWNAEG ELKEDQRKQD IGDVGSLRMV HFGLV UniProtKB: WD repeat-containing and planar cell polarity effector protein fritz homolog |
-Macromolecule #2: Protein inturned
Macromolecule | Name: Protein inturned / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: Mus musculus (house mouse) |
Molecular weight | Theoretical: 107.330539 KDa |
Recombinant expression | Organism: Spodoptera frugiperda (fall armyworm) |
Sequence | String: MGSSHHHHHH SAVDLEVLFQ GPGAGLARGD SRGRPPELPG DLSSQEEEEE EGDSDAGASS LGSYSSASSD TDVEPEWLDS VQKNGELFY LELSEDEEES LLPETQTANH VNHVRFSDKE VIIEEDDSRE RKKSEPKLRR FTKILKSKSL LPRRHHKKSS S NNGPVSIL ...String: MGSSHHHHHH SAVDLEVLFQ GPGAGLARGD SRGRPPELPG DLSSQEEEEE EGDSDAGASS LGSYSSASSD TDVEPEWLDS VQKNGELFY LELSEDEEES LLPETQTANH VNHVRFSDKE VIIEEDDSRE RKKSEPKLRR FTKILKSKSL LPRRHHKKSS S NNGPVSIL KHQSSQKTGV TVQQRYKDVT VYINPRKLTA IKAREQVKLL EVLVGIIHQT KRSWKRSAKQ ADGERLVVHG LL PGGSAMK SGQVLVGDVL VAVNDVDVTS ENIERVLSCI PGPMQVKLTF ENAYAVKRET AQPQKKKAQS STQDLVKLLC GSE ADAVQH STLSIPHISM YLTLQLQSEA AREEQEILYH YPVSEASQKL KSVRGIFLTL CDMLESVTGT QVTSSSLHLN GKQI HVAYL KESDKLLLIG LPAEEVPLPQ LRNMIEDVAQ TLKFMYGSLD SAFCQVENAP RLDHFFSLFF ERALRPGKLH LSGSP SAQQ YAAASAVLLD NLPGVRWLVL PQELKVELDT ALSDLEAADF EELSEDYYDM RRLYTILGSS LFYKGYMVCS HLPKDD VIE IAAYCRQHCL LPLAAKQRIG QLIIWREVFP RHHLQPPSDS DPEAFQEPEG RYFLLVVGLR HYLLCVLLEA GGCASKA TG NPGPDCIYVD QVRATLHQLE GVDSRIEEQL ATSPGPCLSC ADWFLAAPRE KADSLTTSPI LSRLQGPSKT AASPTCRR T FFSDYSFKAR KPSPSRIGGG REPTEGEESA GLSPHATPDA VRKQRESEGS DDNVALLKLA RKKSTLPNPF HLGTSKKEL SEKELEVYDI MKLTSGPENT LFHYVALETV QGIFITPTHE EVAQLGGSVH SQLIKNFHQC CLSIRAFFQQ TLKEEKKKAL SDGEHSEPT NSVSSLSPVK EHGVLFECSP ENWTDQKKTP PVMSYWVVGR LFLNPKPQEL YVCFHDSVSE IAIEMAFKLF F GLTL UniProtKB: Protein inturned |
-Macromolecule #3: Protein fuzzy homolog
Macromolecule | Name: Protein fuzzy homolog / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: Mus musculus (house mouse) |
Molecular weight | Theoretical: 45.542906 KDa |
Recombinant expression | Organism: Spodoptera frugiperda (fall armyworm) |
Sequence | String: MDEGPGSPVH LLCLAASSGV PLFCRSSSGG APSRQQLPFS VIGSLNGVHM FGQNLDVQLN SARTEDTTVV WKNFHDSITL IVLSSEEGT SELRLERMLH MVFGAMVLIV GLEELTNIRN VERLKKELRA SYCLIDSFLG NSELIGDLTQ CVDCVIPPEG S AMQETLSG ...String: MDEGPGSPVH LLCLAASSGV PLFCRSSSGG APSRQQLPFS VIGSLNGVHM FGQNLDVQLN SARTEDTTVV WKNFHDSITL IVLSSEEGT SELRLERMLH MVFGAMVLIV GLEELTNIRN VERLKKELRA SYCLIDSFLG NSELIGDLTQ CVDCVIPPEG S AMQETLSG FAEATGTAFV SLLVSGRVVA ATEGWWRLGM PEAVLLPWLV GSLPPQAARD YPVYLPHGSP TVPHRLLTLT LL RGLELCL LCGPRPPLGQ LDPQLMERWW QPLLEPLRAC LPLGPRALPE GFPLHSDILG LLLLHLELRR CLFTVEPSKD KEP SPEQRR RLLRNFYTLV ATTHFPPEPG PAEKQEDTVY PAQMPRACYL VLGPGMGWQL VAVQLGLRLL LLLLSPHTPT HGLR SLATR TLQALTPLL UniProtKB: Protein fuzzy homolog |
-Macromolecule #4: Ciliogenesis and planar polarity effector 2
Macromolecule | Name: Ciliogenesis and planar polarity effector 2 / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: Mus musculus (house mouse) |
Molecular weight | Theoretical: 28.459801 KDa |
Recombinant expression | Organism: Escherichia coli (E. coli) |
Sequence | String: MARPPMHGSV IVPDWHETVE GKEYLACILR KNRRREFGLL ERPVLPPSVV IDTASYKIFV SGKSGVGKTA LVAKLAGLEV PIVHHETTG IQTTVVFWPA KLKASDCVVM FRFEFWDCGE SALKKFDHML PACKENADAF LFLFSFTDRA SFEDLPGQLT R VAGEAPGL ...String: MARPPMHGSV IVPDWHETVE GKEYLACILR KNRRREFGLL ERPVLPPSVV IDTASYKIFV SGKSGVGKTA LVAKLAGLEV PIVHHETTG IQTTVVFWPA KLKASDCVVM FRFEFWDCGE SALKKFDHML PACKENADAF LFLFSFTDRA SFEDLPGQLT R VAGEAPGL VKIVIGSKFD QYMHTDVPAR DLTAFRQAWE LPLFRVKSVP GRRLADGRTL DGRAGLADTA HVLNGLAEQL WH QDQVAAG LLPSSPESAP G UniProtKB: Ciliogenesis and planar polarity effector 2 |
-Macromolecule #5: GUANOSINE-5'-TRIPHOSPHATE
Macromolecule | Name: GUANOSINE-5'-TRIPHOSPHATE / type: ligand / ID: 5 / Number of copies: 1 / Formula: GTP |
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Molecular weight | Theoretical: 523.18 Da |
Chemical component information | ChemComp-GTP: |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 8 |
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Vitrification | Cryogen name: ETHANE |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 1.04 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: SPOT SCAN / Imaging mode: BRIGHT FIELD |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
-Image processing
Startup model | Type of model: NONE |
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Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 3.35 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 94157 |
Initial angle assignment | Type: MAXIMUM LIKELIHOOD |
Final angle assignment | Type: MAXIMUM LIKELIHOOD |