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- PDB-8qcx: Cryo-EM structure of the inward-facing FLVCR2 -

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Basic information

Entry
Database: PDB / ID: 8qcx
TitleCryo-EM structure of the inward-facing FLVCR2
ComponentsHeme transporter FLVCR2
KeywordsMEMBRANE PROTEIN / MFS / choline transport / human transporter
Function / homology
Function and homology information


heme export / heme transmembrane transporter activity / mitochondrial membrane / heme binding / endoplasmic reticulum membrane / membrane / plasma membrane
Similarity search - Function
: / Major facilitator superfamily / Major Facilitator Superfamily / Major facilitator superfamily domain / Major facilitator superfamily (MFS) profile. / MFS transporter superfamily
Similarity search - Domain/homology
Heme transporter FLVCR2
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.1 Å
AuthorsWeng, T.-H. / Wu, D. / Safarian, S.
Funding support Germany, 1items
OrganizationGrant numberCountry
Max Planck Society Germany
CitationJournal: To Be Published
Title: Cryo-EM structure of the inward-facing FLVCR2
Authors: Weng, T.-H. / Wu, D. / Safarian, S.
History
DepositionAug 28, 2023Deposition site: PDBE / Processing site: PDBE
Revision 1.0Apr 17, 2024Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Heme transporter FLVCR2


Theoretical massNumber of molelcules
Total (without water)58,2771
Polymers58,2771
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: electron microscopy, not applicable
TypeNameSymmetry operationNumber
identity operation1_5551
Buried area0 Å2
ΔGint0 kcal/mol
Surface area18120 Å2
MethodPISA

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Components

#1: Protein Heme transporter FLVCR2 / Calcium-chelate transporter / CCT / Feline leukemia virus subgroup C receptor-related protein 2


Mass: 58277.094 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: FLVCR2, C14orf58 / Cell line (production host): HEK293 / Production host: Homo sapiens (human) / References: UniProt: Q9UPI3

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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

ComponentName: FLVCR2 monomer / Type: COMPLEX / Entity ID: all / Source: RECOMBINANT
Molecular weightValue: 0.058 MDa / Experimental value: YES
Source (natural)Organism: Homo sapiens (human)
Source (recombinant)Organism: Homo sapiens (human) / Cell: HEK293
Buffer solutionpH: 7.4
SpecimenConc.: 1.5 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
Specimen supportGrid material: COPPER / Grid mesh size: 300 divisions/in. / Grid type: Quantifoil R1.2/1.3
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: FLOOD BEAM
Electron lensMode: BRIGHT FIELDBright-field microscopy / Nominal defocus max: 2100 nm / Nominal defocus min: 1100 nm
Image recordingElectron dose: 80 e/Å2 / Film or detector model: FEI FALCON IV (4k x 4k)

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Processing

EM software
IDNameVersionCategory
1RELION3.1particle selection
4RELION3.1CTF correction
7ISOLDEmodel fitting
8Cootmodel fitting
10cryoSPARCinitial Euler assignment
11cryoSPARCfinal Euler assignment
13cryoSPARC3D reconstruction
14PHENIX1.18model refinement
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Particle selectionNum. of particles selected: 3497517
SymmetryPoint symmetry: C1 (asymmetric)
3D reconstructionResolution: 3.1 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 50167 / Algorithm: BACK PROJECTION / Symmetry type: POINT
Atomic model buildingAccession code: AF-Q9UPI3-F1 / Source name: AlphaFold / Type: in silico model
Refine LS restraints
Refine-IDTypeDev idealNumber
ELECTRON MICROSCOPYf_bond_d0.0023365
ELECTRON MICROSCOPYf_angle_d0.454582
ELECTRON MICROSCOPYf_dihedral_angle_d3.574452
ELECTRON MICROSCOPYf_chiral_restr0.035543
ELECTRON MICROSCOPYf_plane_restr0.006555

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