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- EMDB-43163: Unliganded human transthyretin in the compressed conformation -

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ID or keywords:

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Basic information

Entry
Database: EMDB / ID: EMD-43163
TitleUnliganded human transthyretin in the compressed conformation
Map dataApo TTR compressed map
Sample
  • Complex: Transthyretin
    • Protein or peptide: Transthyretin
KeywordsAmyloidosis / TRANSPORT PROTEIN
Function / homology
Function and homology information


Retinoid cycle disease events / thyroid hormone binding / The canonical retinoid cycle in rods (twilight vision) / purine nucleobase metabolic process / Non-integrin membrane-ECM interactions / Retinoid metabolism and transport / hormone activity / azurophil granule lumen / Amyloid fiber formation / Neutrophil degranulation ...Retinoid cycle disease events / thyroid hormone binding / The canonical retinoid cycle in rods (twilight vision) / purine nucleobase metabolic process / Non-integrin membrane-ECM interactions / Retinoid metabolism and transport / hormone activity / azurophil granule lumen / Amyloid fiber formation / Neutrophil degranulation / extracellular space / extracellular exosome / extracellular region / identical protein binding
Similarity search - Function
Transthyretin, conserved site / Transthyretin signature 2. / Transthyretin, thyroxine binding site / Transthyretin signature 1. / Transthyretin / Transthyretin/hydroxyisourate hydrolase / Transthyretin/hydroxyisourate hydrolase domain / Transthyretin/hydroxyisourate hydrolase domain superfamily / HIUase/Transthyretin family
Similarity search - Domain/homology
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.3 Å
AuthorsBasanta B / Nugroho K / Yan N / Kline GM / Tsai FJ / Wu M / Kelly JW / Lander GC
Funding support United States, 2 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)GM142196 United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)AG067594 United States
CitationJournal: To Be Published
Title: The conformational landscape of human transthyretin revealed by cryo-EM
Authors: Basanta B / Nugroho K / Yan N / Kline GM / Powers ET / Tsai FJ / Wu M / Hansel-Harris A / Chen J / Forli S / Kelly JW / Lander GC
History
DepositionDec 18, 2023-
Header (metadata) releaseJun 5, 2024-
Map releaseJun 5, 2024-
UpdateJun 5, 2024-
Current statusJun 5, 2024Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_43163.png

Downloads & links

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Map

FileDownload / File: emd_43163.map.gz / Format: CCP4 / Size: 64 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationApo TTR compressed map
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.56 Å/pix.
x 256 pix.
= 143.872 Å		0.56 Å/pix.
x 256 pix.
= 143.872 Å		0.56 Å/pix.
x 256 pix.
= 143.872 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.562 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.0101
Minimum - Maximum-0.036600396 - 0.0522775
Average (Standard dev.)0.000055871442 (±0.0016812186)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions256256256
Spacing256256256
CellA=B=C: 143.872 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_43163_msk_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Apo TTR compressed half map 1

Fileemd_43163_half_map_1.map
AnnotationApo TTR compressed half map 1
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Apo TTR compressed half map 2

Fileemd_43163_half_map_2.map
AnnotationApo TTR compressed half map 2
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : Transthyretin

EntireName: Transthyretin
Components
  • Complex: Transthyretin
    • Protein or peptide: Transthyretin

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Supramolecule #1: Transthyretin

SupramoleculeName: Transthyretin / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 55.53 KDa

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Macromolecule #1: Transthyretin

MacromoleculeName: Transthyretin / type: protein_or_peptide / ID: 1 / Number of copies: 4 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 13.908557 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
MGPTGTGESK CPLMVKVLDA VRGSPAINVA VHVFRKAADD TWEPFASGKT SESGELHGLT TEEEFVEGIY KVEIDTKSYW KALGISPFH EHAEVVFTAN DSGPRRYTIA ALLSPYSYST TAVVTNPKE

UniProtKB: Transthyretin

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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

Concentration0.85 mg/mL
BufferpH: 7.6
Component:
ConcentrationFormulaName
100.0 mMKClPotassium Chloride
8.66 mMK2HPO4Potassium Phosphate
1.34 mMKH2PO4Potassium Phosphate
1.0 mMC10H16N2O8EDTA
GridModel: UltrAuFoil R1.2/1.3 / Material: GOLD / Mesh: 300 / Support film - Material: GRAPHENE / Support film - topology: CONTINUOUS / Pretreatment - Time: 240 sec. / Pretreatment - Atmosphere: OTHER
Details: The graphene grids were treated with UV/ozone using the UVOCS T10xT10 system. A 10-minute warmup run was performed immediately prior to inserting and treating grids for 4 minutes.
VitrificationCryogen name: ETHANE / Chamber humidity: 90 % / Chamber temperature: 279 K / Instrument: HOMEMADE PLUNGER
Details: 3 uL of sample were applied onto the graphene side of the grid after it was mounted on the plunger (always at the same height), and immediately blotted for 4 seconds by holding a 1 x 6 cm ...Details: 3 uL of sample were applied onto the graphene side of the grid after it was mounted on the plunger (always at the same height), and immediately blotted for 4 seconds by holding a 1 x 6 cm piece of Whatman 1 filter paper parallel to the grid, in full contact. Timing was kept with the help of a metronome. The blotting countdown was started after the blotted liquid spot on the filter paper stopped spreading and the grid was plunged in liquid ethane at the same time the blotting paper was pulled back, in a single motion..

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Electron microscopy

MicroscopeFEI TALOS ARCTICA
TemperatureMin: 78.0 K / Max: 85.0 K
Image recordingFilm or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: COUNTING / Digitization - Dimensions - Width: 3838 pixel / Digitization - Dimensions - Height: 3710 pixel / Number grids imaged: 1 / Number real images: 3739 / Average exposure time: 6.8 sec. / Average electron dose: 52.0 e/Å2
Electron beamAcceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN
Electron opticsC2 aperture diameter: 50.0 µm / Calibrated defocus max: 1.5 µm / Calibrated defocus min: 0.5 µm / Calibrated magnification: 88968 / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 1.5 µm / Nominal defocus min: 0.5 µm / Nominal magnification: 73000
Sample stageSpecimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN
Experimental equipment
Model: Talos Arctica / Image courtesy: FEI Company

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Image processing

Startup modelType of model: PDB ENTRY
PDB model - PDB ID:

1ttr

Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.3 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 3.1) / Number images used: 130181
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD

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