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- PDB-8fh3: Human IFT-A complex structures provide molecular insights into ci... -

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Basic information

Entry
Database: PDB / ID: 8fh3
TitleHuman IFT-A complex structures provide molecular insights into ciliary transport
Components
  • (Intraflagellar transport protein ...) x 2
  • (WD repeat-containing protein ...) x 2
  • Tubby-related protein 3
KeywordsTRANSPORT PROTEIN / IFT-A complex / TULP3 / cilia
Function / homology
Function and homology information


intraciliary transport particle A binding / protein localization to non-motile cilium / intraciliary anterograde transport / intraciliary transport particle A / embryonic body morphogenesis / embryonic heart tube left/right pattern formation / protein localization to ciliary membrane / spinal cord dorsal/ventral patterning / establishment of protein localization to organelle / intraciliary transport ...intraciliary transport particle A binding / protein localization to non-motile cilium / intraciliary anterograde transport / intraciliary transport particle A / embryonic body morphogenesis / embryonic heart tube left/right pattern formation / protein localization to ciliary membrane / spinal cord dorsal/ventral patterning / establishment of protein localization to organelle / intraciliary transport / intraciliary retrograde transport / regulation of cilium assembly / photoreceptor connecting cilium / 9+0 non-motile cilium / embryonic forelimb morphogenesis / embryonic heart tube development / camera-type eye morphogenesis / Intraflagellar transport / protein localization to cilium / non-motile cilium assembly / regulation of G protein-coupled receptor signaling pathway / non-motile cilium / motile cilium / ciliary transition zone / ciliary base / limb development / cilium assembly / photoreceptor outer segment / neural tube closure / axoneme / Hedgehog 'off' state / ciliary tip / phosphatidylinositol-4,5-bisphosphate binding / centriole / phosphatidylinositol binding / negative regulation of smoothened signaling pathway / sperm principal piece / G protein-coupled receptor binding / sperm midpiece / protein-containing complex assembly / cilium / ciliary basal body / protein-macromolecule adaptor activity / intracellular signal transduction / G protein-coupled receptor signaling pathway / centrosome / regulation of DNA-templated transcription / nucleolus / protein-containing complex binding / enzyme binding / extracellular region / nucleoplasm / membrane / nucleus / plasma membrane
Similarity search - Function
Tubby N-terminal / Tubby, C-terminal / Tubby, C-terminal, conserved site / Tub family / Tub family signature 1. / Tub family signature 2. / IFT144, first zinc finger domain / Tubby, N-terminal / Tubby-like, C-terminal / IFT122, C-terminal zinc ribbon domain ...Tubby N-terminal / Tubby, C-terminal / Tubby, C-terminal, conserved site / Tub family / Tub family signature 1. / Tub family signature 2. / IFT144, first zinc finger domain / Tubby, N-terminal / Tubby-like, C-terminal / IFT122, C-terminal zinc ribbon domain / : / IFT122, zinc ribbon domain / WD repeat protein 35 / WDR19, WD40 repeat / WD repeat-containing protein 19/dyf-2 / : / : / : / : / : / : / : / : / WDR19 second beta-propeller / IFT140 first beta-propeller / IFT140 second beta-propeller / WDR19 first beta-propeller / WDR35 second beta-propeller / IF140 C-terminal TPR domain / WDR35/TULP4 N-terminal / WD repeat-containing protein 35, TPR repeats / IFT121-like, TPR repeats / : / : / IFT121, second zinc finger domain / IF140/IFT172 TPR domain / : / IFT80/172/WDR35/WDR19 TPR domain / Intraflagellar transport protein 122 homolog / : / : / IFT122 second beta-propeller / IFT122, TPR domain / : / IFT122 first beta-propeller / Tetratricopeptide-like helical domain superfamily / WD domain, G-beta repeat / Trp-Asp (WD) repeats profile. / Trp-Asp (WD) repeats circular profile. / WD40 repeats / WD40 repeat / WD40-repeat-containing domain superfamily / WD40/YVTN repeat-like-containing domain superfamily
Similarity search - Domain/homology
Tubby-related protein 3 / WD repeat-containing protein 19 / Intraflagellar transport protein 140 homolog / Intraflagellar transport protein 122 homolog / WD repeat-containing protein 35
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 4.3 Å
AuthorsJiang, M. / Palicharla, V.R. / Miller, D. / Hwang, S.H. / Zhu, H. / Hixson, P. / Mukhopadhyay, S. / Sun, J.
Funding support United States, 1items
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 13, 2022Deposition site: RCSB / Processing site: RCSB
Revision 1.0Feb 22, 2023Provider: repository / Type: Initial release
Revision 1.1Apr 12, 2023Group: Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first / _citation.page_last
Revision 1.2Nov 6, 2024Group: Data collection / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / em_admin / pdbx_entry_details / pdbx_modification_feature
Item: _em_admin.last_update / _pdbx_entry_details.has_protein_modification

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: WD repeat-containing protein 35
B: Intraflagellar transport protein 122 homolog
C: WD repeat-containing protein 19
E: Intraflagellar transport protein 140 homolog
I: Tubby-related protein 3
hetero molecules


Theoretical massNumber of molelcules
Total (without water)642,8369
Polymers642,5745
Non-polymers2624
Water00
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_5551

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Components

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WD repeat-containing protein ... , 2 types, 2 molecules AC

#1: Protein WD repeat-containing protein 35 / Intraflagellar transport protein 121 homolog


Mass: 133705.641 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: WDR35, IFT121, KIAA1336 / Production host: Homo sapiens (human) / References: UniProt: Q9P2L0
#3: Protein WD repeat-containing protein 19 / Intraflagellar transport 144 homolog


Mass: 151760.391 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: WDR19, IFT144, KIAA1638 / Production host: Homo sapiens (human) / References: UniProt: Q8NEZ3

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Intraflagellar transport protein ... , 2 types, 2 molecules BE

#2: Protein Intraflagellar transport protein 122 homolog / WD repeat-containing protein 10 / WD repeat-containing protein 140


Mass: 141993.703 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: IFT122, SPG, WDR10, WDR140 / Production host: Homo sapiens (human) / References: UniProt: Q9HBG6
#4: Protein Intraflagellar transport protein 140 homolog / WD and tetratricopeptide repeats protein 2


Mass: 165404.281 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: IFT140, KIAA0590, WDTC2 / Production host: Homo sapiens (human) / References: UniProt: Q96RY7

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Protein / Non-polymers , 2 types, 5 molecules I

#5: Protein Tubby-related protein 3 / Tubby-like protein 3


Mass: 49710.059 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: TULP3, TUBL3 / Production host: Homo sapiens (human) / References: UniProt: O75386
#6: Chemical
ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Zn

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Details

Has ligand of interestN
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

Component
IDNameTypeEntity IDParent-IDSource
1Intraflagellar transport complex A (IFT-A)COMPLEX#1-#50RECOMBINANT
2IFT-A_TULP3COMPLEX1RECOMBINANT
Source (natural)
IDEntity assembly-IDOrganismNcbi tax-ID
21Homo sapiens (human)9606
32Homo sapiens (human)9606
Source (recombinant)
IDEntity assembly-IDOrganismNcbi tax-ID
21Homo sapiens (human)9606
32Homo sapiens (human)9606
Buffer solutionpH: 8
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
VitrificationCryogen name: ETHANE

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: FEI TITAN KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: OTHER
Electron lensMode: BRIGHT FIELD / Nominal defocus max: 2000 nm / Nominal defocus min: 600 nm
Image recordingElectron dose: 53.06 e/Å2 / Film or detector model: GATAN K3 (6k x 4k)

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Processing

CTF correctionType: NONE
3D reconstructionResolution: 4.3 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 113784 / Symmetry type: POINT

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