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Open data
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Basic information
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Title | Cryo-EM structure of dimeric WDR11-FAM91A1 complex | |||||||||||||||||||||
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![]() | Cryo-EM / Vesicle Trafficking / Neural Development / PROTEIN TRANSPORT | |||||||||||||||||||||
Function / homology | ![]() vesicle tethering to Golgi / head development / regulation of smoothened signaling pathway / axoneme / RHOH GTPase cycle / cilium assembly / ciliary basal body / intracellular protein transport / trans-Golgi network / multicellular organism growth ...vesicle tethering to Golgi / head development / regulation of smoothened signaling pathway / axoneme / RHOH GTPase cycle / cilium assembly / ciliary basal body / intracellular protein transport / trans-Golgi network / multicellular organism growth / microtubule cytoskeleton / heart development / cytoplasmic vesicle / lysosomal membrane / membrane / nucleus / cytosol / cytoplasm Similarity search - Function | |||||||||||||||||||||
Biological species | ![]() | |||||||||||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.3 Å | |||||||||||||||||||||
![]() | Jia GW / Deng QH / Su ZM / Jia D | |||||||||||||||||||||
Funding support | ![]()
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![]() | ![]() Title: The WDR11 complex is a receptor for acidic-cluster-containing cargo proteins. Authors: Huaqing Deng / Guowen Jia / Ping Li / Yingying Tang / Lin Zhao / Qin Yang / Jia Zhao / Jinrui Wang / Yingfeng Tu / Xin Yong / Sitao Zhang / Xianming Mo / Daniel D Billadeau / Zhaoming Su / Da Jia / ![]() ![]() Abstract: Vesicle trafficking is a fundamental process that allows for the sorting and transport of specific proteins (i.e., "cargoes") to different compartments of eukaryotic cells. Cargo recognition ...Vesicle trafficking is a fundamental process that allows for the sorting and transport of specific proteins (i.e., "cargoes") to different compartments of eukaryotic cells. Cargo recognition primarily occurs through coats and the associated proteins at the donor membrane. However, it remains unclear whether cargoes can also be selected at other stages of vesicle trafficking to further enhance the fidelity of the process. The WDR11-FAM91A1 complex functions downstream of the clathrin-associated AP-1 complex to facilitate protein transport from endosomes to the TGN. Here, we report the cryo-EM structure of human WDR11-FAM91A1 complex. WDR11 directly and specifically recognizes a subset of acidic clusters, which we term super acidic clusters (SACs). WDR11 complex assembly and its binding to SAC-containing proteins are indispensable for the trafficking of SAC-containing proteins and proper neuronal development in zebrafish. Our studies thus uncover that cargo proteins could be recognized in a sequence-specific manner downstream of a protein coat. | |||||||||||||||||||||
History |
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Structure visualization
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Downloads & links
-EMDB archive
Map data | ![]() | |||
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Header (meta data) | ![]() | |||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8z9mMC ![]() 38300 ![]() 39943 ![]() 39947 ![]() 39949 ![]() 8xfbC ![]() 61078 C: citing same article ( M: atomic model generated by this map |
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Similar structure data | Similarity search - Function & homology ![]() |
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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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Voxel size | X=Y=Z: 0.85 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
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Sample components
-Entire : Cryo-EM structure of dimeric WDR11-FAM91A1 complex
Entire | Name: Cryo-EM structure of dimeric WDR11-FAM91A1 complex |
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Components |
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-Supramolecule #1: Cryo-EM structure of dimeric WDR11-FAM91A1 complex
Supramolecule | Name: Cryo-EM structure of dimeric WDR11-FAM91A1 complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: ![]() |
-Macromolecule #1: Protein FAM91A1
Macromolecule | Name: Protein FAM91A1 / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 95.253234 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MHHHHHHHHM NIDVEFHIRH NYPWNKLPAN VRQSLGNSQR EYEKQVVLYS IRNQLRYRNN LVKHVKKDER RYYEELLKYS RDHLMLYPY HLSDIMVKGL RITPFSYYTG IMEDIMNSEK SYDSLPNFTA ADCLRLLGIG RNQYIDLMNQ CRSSKKFFRR K TARDLLPI ...String: MHHHHHHHHM NIDVEFHIRH NYPWNKLPAN VRQSLGNSQR EYEKQVVLYS IRNQLRYRNN LVKHVKKDER RYYEELLKYS RDHLMLYPY HLSDIMVKGL RITPFSYYTG IMEDIMNSEK SYDSLPNFTA ADCLRLLGIG RNQYIDLMNQ CRSSKKFFRR K TARDLLPI KPVEIAIEAW WVVQAGYITE DDIKICTLPE KCAVDKIIDS GPQLSGSLDY NVVHSLYNKG FIYLDVPISD DS CIAVPPL EGFVMNRVQG DYFETLLYKI FVSIDEHTNV AELANVLEID LSLVKNAVSM YCRLGFAHKK GQVINLDQLH SSW KNVPSV NRLKSTLDPQ KMLLSWDGGE SRSPVQEASS ATDTDTNSQE DPADTASVSS LSLSTGHTKR IAFLFDSTLT AFLM MGNLS PNLKSHAVTM FEVGKLSDES LDSFLIELEK VQSTGEGEAQ RYFDHALTLR NTILFLRHNK DLVAQTAQPD QPNYG FPLD LLRCESLLGL DPATCSRVLN KNYTLLVSMA PLTNEIRPVS SCTPQHIGPA IPEVSSVWFK LYIYHVTGQG PPSLLL SKG TRLRKLPDIF QSYDRLLITS WGHDPGVVPT SNVLTMLNDA LTHSAVLIQG HGLHGIGETV HVPFPFDETE LQGEFTR VN MGVHKALQIL RNRVDLQHLC GYVTMLNASS QLADRKLSDA SDERGEPDLA SGSDVNGSTE SFEMVIEEAT IDSATKQT S GATTEADWVP LELCFGIPLF SSELNRKVCR KIAAHGLCRK ESLQNLLHSS RKLSLQVLNF VHSFQEGASI LDIHTEPSF SSLLSQSSCA DMGVPLPAKN LIFKDGVLSE WSGRSPSSLL IANLHLQ UniProtKB: Protein FAM91A1 |
-Macromolecule #2: WD repeat-containing protein 11
Macromolecule | Name: WD repeat-containing protein 11 / type: protein_or_peptide / ID: 2 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 136.843406 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MLPYTVNFKV SARTLTGALN AHNKAAVDWG WQGLIAYGCH SLVVVIDSIT AQTLQVLEKH KADVVKVKWA RENYHHNIGS PYCLRLASA DVNGKIIVWD VAAGVAQCEI QEHAKPIQDV QWLWNQDASR DLLLAIHPPN YIVLWNADTG TKLWKKSYAD N ILSFSFDP ...String: MLPYTVNFKV SARTLTGALN AHNKAAVDWG WQGLIAYGCH SLVVVIDSIT AQTLQVLEKH KADVVKVKWA RENYHHNIGS PYCLRLASA DVNGKIIVWD VAAGVAQCEI QEHAKPIQDV QWLWNQDASR DLLLAIHPPN YIVLWNADTG TKLWKKSYAD N ILSFSFDP FDPSHLTLLT SEGIVFISDF SPSKPPSGPG KKVYISSPHS SPAHNKLATA TGAKKALNKV KILITQEKPS AE FITLNDC LQLAYLPSKR NHMLLLYPRE ILILDLEVNQ TVGVIAIERT GVPFLQVIPC FQRDGLFCLH ENGCITLRVR RSY NNIFTT SNEEPDPDPV QELTYDLRSQ CDAIRVTKTV RPFSMVCCPV NENAAALVVS DGRVMIWELK SAVCNRNSRN SSSG VSPLY SPVSFCGIPV GVLQNKLPDL SLDNMIGQSA IAGEEHPRGS ILREVHLKFL LTGLLSGLPA PQFAIRMCPP LTTKN IKMY QPLLAVGTSN GSVLVYHLTS GLLHKELSIH SCEVKGIEWT SLTSFLSFAT STPNNMGLVR NELQLVDLPT GRSIAF RGE RGNDESAIEM IKVSHLKQYL AVVFRDKPLE LWDVRTCTLL REMSKNFPTI TALEWSPSHN LKSLRKKQLA TREAMAR QT VVSDTELSIV ESSVISLLQE AESKSELSQN ISAREHFVFT DIDGQVYHLT VEGNSVKDSA RIPPDGSMGS ITCIAWKG D TLVLGDMDGN LNFWDLKGRV SRGIPTHRSW VRKIRFAPGK GNQKLIAMYN DGAEVWDTKE VQMVSSLRSG RNVTFRILD VDWCTSDKVI LASDDGCIRV LEMSMKSACF RMDEQELTEP VWCPYLLVPR ASLALKAFLL HQPWNGQYSL DISHVDYPEN EEIKNLLQE QLNSLSNDIK KLLLDPEFTL LQRCLLVSRL YGDESELHFW TVAAHYLHSL SQEKSASTTA PKEAAPRDKL S NPLDICYD VLCENAYFQK FQLERVNLQE VKRSTYDHTR KCTDQLLLLG QTDRAVQLLL ETSADNQHYY CDSLKACLVT TV TSSGPSQ STIKLVATNM IANGKLAEGV QLLCLIDKAA DACRYLQTYG EWNRAAWLAK VRLNPEECAD VLRRWVDHLC SPQ VNQKSK ALLVLLSLGC FFSVAETLHS MRYFDRAALF VEACLKYGAF EVTEDTEKLI TAIYADYARS LKNLGFKQGA VLFA SKAGA AGKDLLNELE SPKEEPIEE UniProtKB: WD repeat-containing protein 11 |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 8 |
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Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K2 QUANTUM (4k x 4k) / Detector mode: COUNTING / Average electron dose: 58.47 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.992 µm / Nominal defocus min: 0.2 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
Startup model | Type of model: NONE |
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Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 3.3 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 232473 |
Initial angle assignment | Type: MAXIMUM LIKELIHOOD |
Final angle assignment | Type: MAXIMUM LIKELIHOOD |