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- EMDB-29073: Human IFT-A complex structures provide molecular insights into ci... -

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Basic information

Entry
Database: EMDB / ID: EMD-29073
TitleHuman IFT-A complex structures provide molecular insights into ciliary transport
Map data
Sample
  • Complex: Intraflagellar transport complex A (IFT-A)
    • Protein or peptide: WD repeat-containing protein 35
    • Protein or peptide: Intraflagellar transport protein 122 homolog
    • Protein or peptide: WD repeat-containing protein 19
    • Protein or peptide: Tetratricopeptide repeat protein 21B
    • Protein or peptide: Intraflagellar transport protein 140 homolog
    • Protein or peptide: Intraflagellar transport protein 43 homolog
  • Ligand: ZINC ION
KeywordsIFT-A complex / TULP3 / cilia / TRANSPORT PROTEIN
Function / homology
Function and homology information


protein localization to non-motile cilium / smoothened signaling pathway involved in dorsal/ventral neural tube patterning / myotome development / regulation of intraciliary retrograde transport / forebrain dorsal/ventral pattern formation / ear morphogenesis / intraciliary anterograde transport / intraciliary transport particle A / cone photoreceptor outer segment / negative regulation of eating behavior ...protein localization to non-motile cilium / smoothened signaling pathway involved in dorsal/ventral neural tube patterning / myotome development / regulation of intraciliary retrograde transport / forebrain dorsal/ventral pattern formation / ear morphogenesis / intraciliary anterograde transport / intraciliary transport particle A / cone photoreceptor outer segment / negative regulation of eating behavior / digestive system development / embryonic heart tube left/right pattern formation / embryonic body morphogenesis / photoreceptor cell outer segment organization / neural tube patterning / protein localization to ciliary membrane / cerebellar Purkinje cell differentiation / intraciliary retrograde transport / establishment of protein localization to organelle / embryonic camera-type eye development / intraciliary transport / gonad development / spinal cord dorsal/ventral patterning / regulation of cilium assembly / photoreceptor connecting cilium / ciliary tip / ventricular system development / Intraflagellar transport / camera-type eye morphogenesis / embryonic brain development / non-motile cilium assembly / protein localization to cilium / embryonic cranial skeleton morphogenesis / regulation of smoothened signaling pathway / nervous system process / non-motile cilium / embryonic heart tube development / embryonic forelimb morphogenesis / motile cilium / determination of left/right symmetry / embryonic limb morphogenesis / limb development / embryonic digit morphogenesis / smoothened signaling pathway / receptor clustering / axoneme / Bergmann glial cell differentiation / centriolar satellite / photoreceptor outer segment / cilium assembly / Hedgehog 'off' state / negative regulation of smoothened signaling pathway / centriole / ciliary basal body / cellular response to leukemia inhibitory factor / neural tube closure / cell morphogenesis / cilium / microtubule cytoskeleton / positive regulation of canonical Wnt signaling pathway / heart development / protein-containing complex assembly / in utero embryonic development / cytoskeleton / intracellular signal transduction / centrosome / chromatin binding / positive regulation of gene expression / regulation of transcription by RNA polymerase II / membrane / plasma membrane / cytoplasm
Similarity search - Function
Intraflagellar transport protein 43 / Intraflagellar transport protein 43 / Tetratricopeptide repeat protein 21A/21B / WD repeat protein 35 / WDR19, WD40 repeat / WD repeat-containing protein 19/dyf-2 / WD domain, G-beta repeat / Intraflagellar transport protein 122 homolog / Tetratricopeptide repeat / Tetratricopeptide repeat ...Intraflagellar transport protein 43 / Intraflagellar transport protein 43 / Tetratricopeptide repeat protein 21A/21B / WD repeat protein 35 / WDR19, WD40 repeat / WD repeat-containing protein 19/dyf-2 / WD domain, G-beta repeat / Intraflagellar transport protein 122 homolog / Tetratricopeptide repeat / Tetratricopeptide repeat / Anaphase-promoting complex subunit 4, WD40 domain / Anaphase-promoting complex subunit 4 WD40 domain / Tetratricopeptide repeat / TPR repeat region circular profile. / TPR repeat profile. / Tetratricopeptide repeats / Tetratricopeptide repeat / Tetratricopeptide-like helical domain superfamily / Trp-Asp (WD) repeats profile. / Trp-Asp (WD) repeats circular profile. / WD domain, G-beta repeat / WD40 repeats / WD40 repeat / WD40-repeat-containing domain superfamily / WD40/YVTN repeat-like-containing domain superfamily
Similarity search - Domain/homology
Tetratricopeptide repeat protein 21B / WD repeat-containing protein 19 / Intraflagellar transport protein 43 homolog / Intraflagellar transport protein 140 homolog / Intraflagellar transport protein 122 homolog / WD repeat-containing protein 35
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.7 Å
AuthorsJiang M / Palicharla VR / Miller D / Hwang SH / Zhu H / Hixson P / Mukhopadhyay S / Sun J
Funding support United States, 1 items
OrganizationGrant numberCountry
National Institutes of Health/National Heart, Lung, and Blood Institute (NIH/NHLBI)R00HL143037 United States
CitationJournal: Cell Res / Year: 2023
Title: Human IFT-A complex structures provide molecular insights into ciliary transport.
Authors: Meiqin Jiang / Vivek Reddy Palicharla / Darcie Miller / Sun-Hee Hwang / Hanwen Zhu / Patricia Hixson / Saikat Mukhopadhyay / Ji Sun /
Abstract: Intraflagellar transport (IFT) complexes, IFT-A and IFT-B, form bidirectional trains that move along the axonemal microtubules and are essential for assembling and maintaining cilia. Mutations in IFT ...Intraflagellar transport (IFT) complexes, IFT-A and IFT-B, form bidirectional trains that move along the axonemal microtubules and are essential for assembling and maintaining cilia. Mutations in IFT subunits lead to numerous ciliopathies involving multiple tissues. However, how IFT complexes assemble and mediate cargo transport lacks mechanistic understanding due to missing high-resolution structural information of the holo-complexes. Here we report cryo-EM structures of human IFT-A complexes in the presence and absence of TULP3 at overall resolutions of 3.0-3.9 Å. IFT-A adopts a "lariat" shape with interconnected core and peripheral subunits linked by structurally vital zinc-binding domains. TULP3, the cargo adapter, interacts with IFT-A through its N-terminal region, and interface mutations disrupt cargo transport. We also determine the molecular impacts of disease mutations on complex formation and ciliary transport. Our work reveals IFT-A architecture, sheds light on ciliary transport and IFT train formation, and enables the rationalization of disease mutations in ciliopathies.
History
DepositionDec 12, 2022-
Header (metadata) releaseFeb 22, 2023-
Map releaseFeb 22, 2023-
UpdateNov 13, 2024-
Current statusNov 13, 2024Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_29073.png

Downloads & links

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Map

FileDownload / File: emd_29073.map.gz / Format: CCP4 / Size: 421.9 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

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AxesZ (Sec.)Y (Row.)X (Col.)
1.48 Å/pix.
x 480 pix.
= 710.4 Å		1.48 Å/pix.
x 480 pix.
= 710.4 Å		1.48 Å/pix.
x 480 pix.
= 710.4 Å

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Images are generated by Spider.

Voxel sizeX=Y=Z: 1.48 Å
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Contour LevelBy AUTHOR: 1.0
Minimum - Maximum-0.16661645 - 6.052928
Average (Standard dev.)0.026118577 (±0.072787926)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions480480480
Spacing480480480
CellA=B=C: 710.4 Å
α=β=γ: 90.0 °

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Supplemental data

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Additional map: #4

Fileemd_29073_additional_1.map
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Additional map: #3

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Additional map: #2

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Additional map: #1

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Half map: #2

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Sample components

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Entire : Intraflagellar transport complex A (IFT-A)

EntireName: Intraflagellar transport complex A (IFT-A)
Components
  • Complex: Intraflagellar transport complex A (IFT-A)
    • Protein or peptide: WD repeat-containing protein 35
    • Protein or peptide: Intraflagellar transport protein 122 homolog
    • Protein or peptide: WD repeat-containing protein 19
    • Protein or peptide: Tetratricopeptide repeat protein 21B
    • Protein or peptide: Intraflagellar transport protein 140 homolog
    • Protein or peptide: Intraflagellar transport protein 43 homolog
  • Ligand: ZINC ION

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Supramolecule #1: Intraflagellar transport complex A (IFT-A)

SupramoleculeName: Intraflagellar transport complex A (IFT-A) / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#6
Source (natural)Organism: Homo sapiens (human)

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Macromolecule #1: WD repeat-containing protein 35

MacromoleculeName: WD repeat-containing protein 35 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 133.705641 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MFFYLSKKIS IPNNVKLQCV SWNKEQGFIA CGGEDGLLKV LKLETQTDDA KLRGLAAPSN LSMNQTLEGH SGSVQVVTWN EQYQKLTTS DENGLIIVWM LYKGSWIEEM INNRNKSVVR SMSWNADGQK ICIVYEDGAV IVGSVDGNRI WGKDLKGIQL S HVTWSADS ...String:
MFFYLSKKIS IPNNVKLQCV SWNKEQGFIA CGGEDGLLKV LKLETQTDDA KLRGLAAPSN LSMNQTLEGH SGSVQVVTWN EQYQKLTTS DENGLIIVWM LYKGSWIEEM INNRNKSVVR SMSWNADGQK ICIVYEDGAV IVGSVDGNRI WGKDLKGIQL S HVTWSADS KVLLFGMANG EIHIYDNQGN FMIKMKLSCL VNVTGAISIA GIHWYHGTEG YVEPDCPCLA VCFDNGRCQI MR HENDQNP VLIDTGMYVV GIQWNHMGSV LAVAGFQKAA MQDKDVNIVQ FYTPFGEHLG TLKVPGKEIS ALSWEGGGLK IAL AVDSFI YFANIRPNYK WGYCSNTVVY AYTRPDRPEY CVVFWDTKNN EKYVKYVKGL ISITTCGDFC ILATKADENH PQEE NEMET FGATFVLVLC NSIGTPLDPK YIDIVPLFVA MTKTHVIAAS KEAFYTWQYR VAKKLTALEI NQITRSRKEG RERIY HVDD TPSGSMDGVL DYSKTIQGTR DPICAITASD KILIVGRESG TIQRYSLPNV GLIQKYSLNC RAYQLSLNCN SSRLAI IDI SGVLTFFDLD ARVTDSTGQQ VVGELLKLER RDVWDMKWAK DNPDLFAMME KTRMYVFRNL DPEEPIQTSG YICNFED LE IKSVLLDEIL KDPEHPNKDY LINFEIRSLR DSRALIEKVG IKDASQFIED NPHPRLWRLL AEAALQKLDL YTAEQAFV R CKDYQGIKFV KRLGKLLSES MKQAEVVGYF GRFEEAERTY LEMDRRDLAI GLRLKLGDWF RVLQLLKTGS GDADDSLLE QANNAIGDYF ADRQKWLNAV QYYVQGRNQE RLAECYYMLE DYEGLENLAI SLPENHKLLP EIAQMFVRVG MCEQAVTAFL KCSQPKAAV DTCVHLNQWN KAVELAKNHS MKEIGSLLAR YASHLLEKNK TLDAIELYRK ANYFFDAAKL MFKIADEEAK K GSKPLRVK KLYVLSALLI EQYHEQMKNA QRGKVKGKSS EATSALAGLL EEEVLSTTDR FTDNAWRGAE AYHFFILAQR QL YEGCVDT ALKTALHLKD YEDIIPPVEI YSLLALCACA SRAFGTCSKA FIKLKSLETL SSEQKQQYED LALEIFTKHT SKD NRKPEL DSLMEGGEGK LPTCVATGSP ITEYQFWMCS VCKHGVLAQE ISHYSFCPLC HSPVG

UniProtKB: WD repeat-containing protein 35

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Macromolecule #2: Intraflagellar transport protein 122 homolog

MacromoleculeName: Intraflagellar transport protein 122 homolog / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 141.993703 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MRAVLTWRDK AEHCINDIAF KPDGTQLILA AGSRLLVYDT SDGTLLQPLK GHKDTVYCVA YAKDGKRFAS GSADKSVIIW TSKLEGILK YTHNDAIQCV SYNPITHQLA SCSSSDFGLW SPEQKSVSKH KSSSKIICCS WTNDGQYLAL GMFNGIISIR N KNGEEKVK ...String:
MRAVLTWRDK AEHCINDIAF KPDGTQLILA AGSRLLVYDT SDGTLLQPLK GHKDTVYCVA YAKDGKRFAS GSADKSVIIW TSKLEGILK YTHNDAIQCV SYNPITHQLA SCSSSDFGLW SPEQKSVSKH KSSSKIICCS WTNDGQYLAL GMFNGIISIR N KNGEEKVK IERPGGSLSP IWSICWNPSS RWESFWMNRE NEDAEDVIVN RYIQEIPSTL KSAVYSSQGS EAEEEEPEED DD SPRDDNL EERNDILAVA DWGQKVSFYQ LSGKQIGKDR ALNFDPCCIS YFTKGEYILL GGSDKQVSLF TKDGVRLGTV GEQ NSWVWT CQAKPDSNYV VVGCQDGTIS FYQLIFSTVH GLYKDRYAYR DSMTDVIVQH LITEQKVRIK CKELVKKIAI YRNR LAIQL PEKILIYELY SEDLSDMHYR VKEKIIKKFE CNLLVVCANH IILCQEKRLQ CLSFSGVKER EWQMESLIRY IKVIG GPPG REGLLVGLKN GQILKIFVDN LFAIVLLKQA TAVRCLDMSA SRKKLAVVDE NDTCLVYDID TKELLFQEPN ANSVAW NTQ CEDMLCFSGG GYLNIKASTF PVHRQKLQGF VVGYNGSKIF CLHVFSISAV EVPQSAPMYQ YLDRKLFKEA YQIACLG VT DTDWRELAME ALEGLDFETA KKAFIRVQDL RYLELISSIE ERKKRGETNN DLFLADVFSY QGKFHEAAKL YKRSGHEN L ALEMYTDLCM FEYAKDFLGS GDPKETKMLI TKQADWARNI KEPKAAVEMY ISAGEHVKAI EICGDHGWVD MLIDIARKL DKAEREPLLL CATYLKKLDS PGYAAETYLK MGDLKSLVQL HVETQRWDEA FALGEKHPEF KDDIYMPYAQ WLAENDRFEE AQKAFHKAG RQREAVQVLE QLTNNAVAES RFNDAAYYYW MLSMQCLDIA QDPAQKDTML GKFYHFQRLA ELYHGYHAIH R HTEDPFSV HRPETLFNIS RFLLHSLPKD TPSGISKVKI LFTLAKQSKA LGAYRLARHA YDKLRGLYIP ARFQKSIELG TL TIRAKPF HDSEELVPLC YRCSTNNPLL NNLGNVCINC RQPFIFSASS YDVLHLVEFY LEEGITDEEA ISLIDLEVLR PKR DDRQLE IANNSSQILR LVETKDSIGD EDPFTAKLSF EQGGSEFVPV VVSRLVLRSM SRRDVLIKRW PPPLRWQYFR SLLP DASIT MCPSCFQMFH SEDYELLVLQ HGCCPYCRRC KDDPGP

UniProtKB: Intraflagellar transport protein 122 homolog

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Macromolecule #3: WD repeat-containing protein 19

MacromoleculeName: WD repeat-containing protein 19 / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 151.760391 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MKRIFSLLEK TWLGAPIQFA WQKTSGNYLA VTGADYIVKI FDRHGQKRSE INLPGNCVAM DWDKDGDVLA VIAEKSSCIY LWDANTNKT SQLDNGMRDQ MSFLLWSKVG SFLAVGTVKG NLLIYNHQTS RKIPVLGKHT KRITCGCWNA ENLLALGGED K MITVSNQE ...String:
MKRIFSLLEK TWLGAPIQFA WQKTSGNYLA VTGADYIVKI FDRHGQKRSE INLPGNCVAM DWDKDGDVLA VIAEKSSCIY LWDANTNKT SQLDNGMRDQ MSFLLWSKVG SFLAVGTVKG NLLIYNHQTS RKIPVLGKHT KRITCGCWNA ENLLALGGED K MITVSNQE GDTIRQTQVR SEPSNMQFFL MKMDDRTSAA ESMISVVLGK KTLFFLNLNE PDNPADLEFQ QDFGNIVCYN WY GDGRIMI GFSCGHFVVI STHTGELGQE IFQARNHKDN LTSIAVSQTL NKVATCGDNC IKIQDLVDLK DMYVILNLDE ENK GLGTLS WTDDGQLLAL STQRGSLHVF LTKLPILGDA CSTRIAYLTS LLEVTVANPV EGELPITVSV DVEPNFVAVG LYHL AVGMN NRAWFYVLGE NAVKKLKDME YLGTVASICL HSDYAAALFE GKVQLHLIES EILDAQEERE TRLFPAVDDK CRILC HALT SDFLIYGTDT GVVQYFYIED WQFVNDYRHP VSVKKIFPDP NGTRLVFIDE KSDGFVYCPV NDATYEIPDF SPTIKG VLW ENWPMDKGVF IAYDDDKVYT YVFHKDTIQG AKVILAGSTK VPFAHKPLLL YNGELTCQTQ SGKVNNIYLS THGFLSN LK DTGPDELRPM LAQNLMLKRF SDAWEMCRIL NDEAAWNELA RACLHHMEVE FAIRVYRRIG NVGIVMSLEQ IKGIEDYN L LAGHLAMFTN DYNLAQDLYL ASSCPIAALE MRRDLQHWDS ALQLAKHLAP DQIPFISKEY AIQLEFAGDY VNALAHYEK GITGDNKEHD EACLAGVAQM SIRMGDIRRG VNQALKHPSR VLKRDCGAIL ENMKQFSEAA QLYEKGLYYD KAASVYIRSK NWAKVGDLL PHVSSPKIHL QYAKAKEADG RYKEAVVAYE NAKQWQSVIR IYLDHLNNPE KAVNIVRETQ SLDGAKMVAR F FLQLGDYG SAIQFLVMSK CNNEAFTLAQ QHNKMEIYAD IIGSEDTTNE DYQSIALYFE GEKRYLQAGK FFLLCGQYSR AL KHFLKCP SSEDNVAIEM AIETVGQAKD ELLTNQLIDH LLGENDGMPK DAKYLFRLYM ALKQYREAAQ TAIIIAREEQ SAG NYRNAH DVLFSMYAEL KSQKIKIPSE MATNLMILHS YILVKIHVKN GDHMKGARML IRVANNISKF PSHIVPILTS TVIE CHRAG LKNSAFSFAA MLMRPEYRSK IDAKYKKKIE GMVRRPDISE IEEATTPCPF CKFLLPECEL LCPGCKNSIP YCIAT GRHM LKDDWTVCPH CDFPALYSEL KIMLNTESTC PMCSERLNAA QLKKISDCTQ YLRTEEEL

UniProtKB: WD repeat-containing protein 19

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Macromolecule #4: Tetratricopeptide repeat protein 21B

MacromoleculeName: Tetratricopeptide repeat protein 21B / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 151.137438 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MDSQELKTLI NYYCQERYFH HVLLVASEGI KRYGSDPVFR FYHAYGTLME GKTQEALREF EAIKNKQDVS LCSLLALIYA HKMSPNPDR EAILESDARV KEQRKGAGEK ALYHAGLFLW HIGRHDKARE YIDRMIKISD GSKQGHVLKA WLDITRGKEP Y TKKALKYF ...String:
MDSQELKTLI NYYCQERYFH HVLLVASEGI KRYGSDPVFR FYHAYGTLME GKTQEALREF EAIKNKQDVS LCSLLALIYA HKMSPNPDR EAILESDARV KEQRKGAGEK ALYHAGLFLW HIGRHDKARE YIDRMIKISD GSKQGHVLKA WLDITRGKEP Y TKKALKYF EEGLQDGNDT FALLGKAQCL EMRQNYSGAL ETMNQIIVNF PSFLPAFVKK MKLQLALQDW DQTVETAQRL LL QDSQNVE ALRMQALYYV CREGDIEKAS TKLENLGNAL DAMEPQNAQL FYNITLAFSR TCGRSQLILQ KIQTLLERAF SLN PQQSEF ATELGYQMIL QGRVKEALKW YKTAMTLDET SVSALVGFIQ CQLIEGQLQD ADQQLEFLNE IQQSIGKSAE LIYL HAVLA MKKNKRQEEV INLLNDVLDT HFSQLEGLPL GIQYFEKLNP DFLLEIVMEY LSFCPMQPAS PGQPLCPLLR RCISV LETV VRTVPGLLQT VFLIAKVKYL SGDIEAAFNN LQHCLEHNPS YADAHLLLAQ VYLSQEKVKL CSQSLELCLS YDFKVR DYP LYHLIKAQSQ KKMGEIADAI KTLHMAMSLP GMKRIGASTK SKDRKTEVDT SHRLSIFLEL IDVHRLNGEQ HEATKVL QD AIHEFSGTSE EVRVTIANAD LALAQGDIER ALSILQNVTA EQPYFIEARE KMADIYLKHR KDKMLYITCF REIAERMA N PRSFLLLGDA YMNILEPEEA IVAYEQALNQ NPKDGTLASK MGKALIKTHN YSMAITYYEA ALKTGQKNYL CYDLAELLL KLKWYDKAEK VLQHALAHEP VNELSALMED GRCQVLLAKV YSKMEKLGDA ITALQQAREL QARVLKRVQM EQPDAVPAQK HLAAEICAE IAKHSVAQRD YEKAIKFYRE ALVHCETDNK IMLELARLYL AQDDPDSCLR QCALLLQSDQ DNEAATMMMA D LMFRKQDY EQAVFHLQQL LERKPDNYMT LSRLIDLLRR CGKLEDVPRF FSMAEKRNSR AKLEPGFQYC KGLYLWYTGE PN DALRHFN KARKDRDWGQ NALYNMIEIC LNPDNETVGG EVFENLDGDL GNSTEKQESV QLAVRTAEKL LKELKPQTVQ GHV QLRIME NYCLMATKQK SNVEQALNTF TEIAASEKEH IPALLGMATA YMILKQTPRA RNQLKRIAKM NWNAIDAEEF EKSW LLLAD IYIQSAKYDM AEDLLKRCLR HNRSCCKAYE YMGYIMEKEQ AYTDAALNYE MAWKYSNRTN PAVGYKLAFN YLKAK RYVD SIDICHQVLE AHPTYPKIRK DILDKARASL RP

UniProtKB: Tetratricopeptide repeat protein 21B

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Macromolecule #5: Intraflagellar transport protein 140 homolog

MacromoleculeName: Intraflagellar transport protein 140 homolog / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 165.404281 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MALYYDHQIE APDAAGSPSF ISWHPVHPFL AVAYISTTST GSVDIYLEQG ECVPDTHVER PFRVASLCWH PTRLVLAVGW ETGEVTVFN KQDKEQHTMP LTHTADITVL RWSPSGNCLL SGDRLGVLLL WRLDQRGRVQ GTPLLKHEYG KHLTHCIFRL P PPGEDLVQ ...String:
MALYYDHQIE APDAAGSPSF ISWHPVHPFL AVAYISTTST GSVDIYLEQG ECVPDTHVER PFRVASLCWH PTRLVLAVGW ETGEVTVFN KQDKEQHTMP LTHTADITVL RWSPSGNCLL SGDRLGVLLL WRLDQRGRVQ GTPLLKHEYG KHLTHCIFRL P PPGEDLVQ LAKAAVSGDE KALDMFNWKK SSSGSLLKMG SHEGLLFFVS LMDGTVHYVD EKGKTTQVVS ADSTIQMLFY ME KREALVV VTENLRLSLY TVPPEGKAEE VMKVKLSGKT GRRADIALIE GSLLVMAVGE AALRFWDIER GENYILSPDE KFG FEKGEN MNCVCYCKVK GLLAAGTDRG RVAMWRKVPD FLGSPGAEGK DRWALQTPTE LQGNITQIQW GSRKNLLAVN SVIS VAILS ERAMSSHFHQ QVAAMQVSPS LLNVCFLSTG VAHSLRTDMH ISGVFATKDA VAVWNGRQVA IFELSGAAIR SAGTF LCET PVLAMHEENV YTVESNRVQV RTWQGTVKQL LLFSETEGNP CFLDICGNFL VVGTDLAHFK SFDLSRREAK AHCSCR SLA ELVPGVGGIA SLRCSSSGST ISILPSKADN SPDSKICFYD VEMDTVTVFD FKTGQIDRRE TLSFNEQETN KSHLFVD EG LKNYVPVNHF WDQSEPRLFV CEAVQETPRS QPQSANGQPQ DGRAGPAADV LILSFFISEE HGFLLHESFP RPATSHSL L GMEVPYYYFT RKPEEADRED EVEPGCHHIP QMVSRRPLRD FVGLEDCDKA TRDAMLHFSF FVTIGDMDEA FKSIKLIKS EAVWENMARM CVKTQRLDVA KVCLGNMGHA RGARALREAE QEPELEARVA VLATQLGMLE DAEQLYRKCK RHDLLNKFYQ AAGRWQEAL QVAEHHDRVH LRSTYHRYAG HLEASADCSR ALSYYEKSDT HRFEVPRMLS EDLPSLELYV NKMKDKTLWR W WAQYLESQ GEMDAALHYY ELARDHFSLV RIHCFQGNVQ KAAQIANETG NLAASYHLAR QYESQEEVGQ AVHFYTRAQA FK NAIRLCK ENGLDDQLMN LALLSSPEDM IEAARYYEEK GVQMDRAVML YHKAGHFSKA LELAFATQQF VALQLIAEDL DET SDPALL ARCSDFFIEH SQYERAVELL LAARKYQEAL QLCLGQNMSI TEEMAEKMTV AKDSSDLPEE SRRELLEQIA DCCM RQGSY HLATKKYTQA GNKLKAMRAL LKSGDTEKIT FFASVSRQKE IYIMAANYLQ SLDWRKEPEI MKNIIGFYTK GRALD LLAG FYDACAQVEI DEYQNYDKAH GALTEAYKCL AKAKAKSPLD QETRLAQLQS RMALVKRFIQ ARRTYTEDPK ESIKQC ELL LEEPDLDSTI RIGDVYGFLV EHYVRKEEYQ TAYRFLEEMR RRLPLANMSY YVSPQAVDAV HRGLGLPLPR TVPEQVR HN SMEDARELDE EVVEEADDDP

UniProtKB: Intraflagellar transport protein 140 homolog

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Macromolecule #6: Intraflagellar transport protein 43 homolog

MacromoleculeName: Intraflagellar transport protein 43 homolog / type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 23.55807 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MEDLLDLDEE LRYSLATSRA KMGRRAQQES AQAENHLNGK NSSLTLTGET SSAKLPRCRQ GGWAGDSVKA SKFRRKASEE IEDFRLRPQ SLNGSDYGGD IPIIPDLEEV QEEDFVLQVA APPSIQIKRV MTYRDLDNDL MKYSAIQTLD GEIDLKLLTK V LAPEHEVR ...String:
MEDLLDLDEE LRYSLATSRA KMGRRAQQES AQAENHLNGK NSSLTLTGET SSAKLPRCRQ GGWAGDSVKA SKFRRKASEE IEDFRLRPQ SLNGSDYGGD IPIIPDLEEV QEEDFVLQVA APPSIQIKRV MTYRDLDNDL MKYSAIQTLD GEIDLKLLTK V LAPEHEVR EDDVGWDWDH LFTEVSSEVL TEWDPLQTEK EDPAGQARHT

UniProtKB: Intraflagellar transport protein 43 homolog

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Macromolecule #7: ZINC ION

MacromoleculeName: ZINC ION / type: ligand / ID: 7 / Number of copies: 5 / Formula: ZN
Molecular weightTheoretical: 65.409 Da

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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

BufferpH: 8
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 66.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: OTHER / Imaging mode: OTHER / Nominal defocus max: 2.0 µm / Nominal defocus min: 0.8 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Startup modelType of model: NONE
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.7 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 67560
Initial angle assignmentType: OTHER
Final angle assignmentType: OTHER

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