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- EMDB-28536: FAM46C/BCCIPalpha/Nanobody complex -

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Open data


ID or keywords:

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Basic information

Entry
Database: EMDB / ID: EMD-28536
TitleFAM46C/BCCIPalpha/Nanobody complex
Map data
Sample
  • Complex: the complex between FAM46C and BCCIPalpha
    • Protein or peptide: Synthetic nanobody 1
    • Protein or peptide: Terminal nucleotidyltransferase 5C
    • Protein or peptide: Isoform 2 of BRCA2 and CDKN1A-interacting protein
Function / homology
Function and homology information


mRNA stabilization / polynucleotide adenylyltransferase / poly(A) RNA polymerase activity / negative regulation of cell differentiation / in utero embryonic development / centrosome / RNA binding / nucleoplasm / nucleus / cytoplasm
Similarity search - Function
Terminal nucleotidyltransferase / Domain of unknown function (DUF1693) / Nucleotidyltransferase
Similarity search - Domain/homology
Terminal nucleotidyltransferase 5C / Isoform 2 of BRCA2 and CDKN1A-interacting protein
Similarity search - Component
Biological speciesHomo sapiens (human) / Lama glama (llama)
Methodsingle particle reconstruction / cryo EM / Resolution: 6.5 Å
AuthorsLiu S / Chen H / Yin Y / Bai X / Zhang X
Funding support United States, 4 items
OrganizationGrant numberCountry
National Institutes of Health/National Cancer Institute (NIH/NCI)R01CA220283 United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)R01GM143158 United States
Welch FoundationI-1702 United States
Welch FoundationI-1944 United States
CitationJournal: Sci Adv / Year: 2023
Title: Inhibition of FAM46/TENT5 activity by BCCIPα adopting a unique fold.
Authors: Shun Liu / Hua Chen / Yan Yin / Defen Lu / Guoming Gao / Jie Li / Xiao-Chen Bai / Xuewu Zhang /
Abstract: The FAM46 (also known as TENT5) proteins are noncanonical poly(A) polymerases (PAPs) implicated in regulating RNA stability. The regulatory mechanisms of FAM46 are poorly understood. Here, we report ...The FAM46 (also known as TENT5) proteins are noncanonical poly(A) polymerases (PAPs) implicated in regulating RNA stability. The regulatory mechanisms of FAM46 are poorly understood. Here, we report that the nuclear protein BCCIPα, but not the alternatively spliced isoform BCCIPβ, binds FAM46 and inhibits their PAP activity. Unexpectedly, our structures of the FAM46A/BCCIPα and FAM46C/BCCIPα complexes show that, despite sharing most of the sequence and differing only at the C-terminal portion, BCCIPα adopts a unique structure completely different from BCCIPβ. The distinct C-terminal segment of BCCIPα supports the adoption of the unique fold but does not directly interact with FAM46. The β sheets in BCCIPα and FAM46 pack side by side to form an extended β sheet. A helix-loop-helix segment in BCCIPα inserts into the active site cleft of FAM46, thereby inhibiting the PAP activity. Our results together show that the unique fold of BCCIPα underlies its interaction with and functional regulation of FAM46.
History
DepositionOct 7, 2022-
Header (metadata) releaseMar 15, 2023-
Map releaseMar 15, 2023-
UpdateApr 26, 2023-
Current statusApr 26, 2023Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_28536.png

Downloads & links

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Map

FileDownload / File: emd_28536.map.gz / Format: CCP4 / Size: 30.5 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Voxel sizeX=Y=Z: 1.08 Å
Density
Contour LevelBy AUTHOR: 0.014
Minimum - Maximum-0.0062977304 - 0.031955514
Average (Standard dev.)0.00064989395 (±0.002662233)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions200200200
Spacing200200200
CellA=B=C: 216.00002 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: #2

Fileemd_28536_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: #1

Fileemd_28536_half_map_2.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : the complex between FAM46C and BCCIPalpha

EntireName: the complex between FAM46C and BCCIPalpha
Components
  • Complex: the complex between FAM46C and BCCIPalpha
    • Protein or peptide: Synthetic nanobody 1
    • Protein or peptide: Terminal nucleotidyltransferase 5C
    • Protein or peptide: Isoform 2 of BRCA2 and CDKN1A-interacting protein

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Supramolecule #1: the complex between FAM46C and BCCIPalpha

SupramoleculeName: the complex between FAM46C and BCCIPalpha / type: complex / ID: 1 / Chimera: Yes / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 300 KDa

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Macromolecule #1: Synthetic nanobody 1

MacromoleculeName: Synthetic nanobody 1 / type: protein_or_peptide / ID: 1 / Number of copies: 4 / Enantiomer: LEVO
Source (natural)Organism: Lama glama (llama)
Molecular weightTheoretical: 13.719396 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
GPHMQVQLQE SGGGLVQAGG SLRLSCAASG TISPRGVMGW YRQAPGKERE FVAAINYGGT TYYADSVKGR FTISRDNAKN TVYLQMNSL KPEDTAVYYC AVYYYINSQR KVLLYWGQGT QVTVSS

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Macromolecule #2: Terminal nucleotidyltransferase 5C

MacromoleculeName: Terminal nucleotidyltransferase 5C / type: protein_or_peptide / ID: 2 / Number of copies: 4 / Enantiomer: LEVO / EC number: polynucleotide adenylyltransferase
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 24.533254 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: GPGAPSVLNW DQVSRLHEVL TEVVPIHGRG NFPTLEITLK DIVQTVRSRL EEAGIKVHDV RLNGSAAGHV LVKDNGLGCK DLDLIFHVA LPTEAEFQLV RDVVLCSLLN FLPEGVNKLK ISPVTLKEAY VQKLVKVCTD TDRWSLISLS NKNGKNVQLK F VDSIRRQF ...String:
GPGAPSVLNW DQVSRLHEVL TEVVPIHGRG NFPTLEITLK DIVQTVRSRL EEAGIKVHDV RLNGSAAGHV LVKDNGLGCK DLDLIFHVA LPTEAEFQLV RDVVLCSLLN FLPEGVNKLK ISPVTLKEAY VQKLVKVCTD TDRWSLISLS NKNGKNVQLK F VDSIRRQF EFSVDSFQII LDSLLFFYDC SNNPISEHFH PTVIGES(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)

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Macromolecule #3: Isoform 2 of BRCA2 and CDKN1A-interacting protein

MacromoleculeName: Isoform 2 of BRCA2 and CDKN1A-interacting protein / type: protein_or_peptide / ID: 3 / Number of copies: 4 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 28.190066 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: GPGAPDEVID EEVNIEFEAY SLSDNDYDGI KKLLQQLFLK APVNTAELTD LLIQQNHIGS VIKQTDVEVF GFISLLNLTE RKGTQCVEQ IQELVLRFCE KNCEKSMVEQ LDKFLNDTTK PVGLLLSERF INVPPQIALP MYQQLQKELA GAHRTNKPCG K CYFYLLIS ...String:
GPGAPDEVID EEVNIEFEAY SLSDNDYDGI KKLLQQLFLK APVNTAELTD LLIQQNHIGS VIKQTDVEVF GFISLLNLTE RKGTQCVEQ IQELVLRFCE KNCEKSMVEQ LDKFLNDTTK PVGLLLSERF INVPPQIALP MYQQLQKELA GAHRTNKPCG K CYFYLLIS KTFVEAGKNN SAALMFANAE EEFFYEEQGK PEVLGGPDTR PVPIQHNGGS RGQVTALVSL KAGLIQSRST LS DFQGTFM TVGIALS

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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: 7.5
VitrificationCryogen name: NITROGEN

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy / Nominal defocus max: 2.5 µm / Nominal defocus min: 1.5 µm
Image recordingFilm or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 60.0 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
Final reconstructionResolution.type: BY AUTHOR / Resolution: 6.5 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 7376
FSC plot (resolution estimation)

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