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- EMDB-39773: Cryo-EM structure of E.coli SPFH-NfeD family protein complex QmcA-YbbJ -

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Basic information

Entry
Database: EMDB / ID: EMD-39773
TitleCryo-EM structure of E.coli SPFH-NfeD family protein complex QmcA-YbbJ
Map data
Sample
  • Complex: QmcA-YbbJ complex
    • Protein or peptide: Protein QmcA
    • Protein or peptide: Inner membrane protein YbbJ
Keywordscomplex / MEMBRANE PROTEIN
Function / homology
Function and homology information


identical protein binding / plasma membrane
Similarity search - Function
: / Band 7/stomatin-like, conserved site / Band 7 protein family signature. / NfeD-like, C-terminal domain / : / NfeD-like C-terminal, partner-binding / Stomatin/HflK/HflC family / Band 7 domain / SPFH domain / Band 7 family / prohibitin homologues ...: / Band 7/stomatin-like, conserved site / Band 7 protein family signature. / NfeD-like, C-terminal domain / : / NfeD-like C-terminal, partner-binding / Stomatin/HflK/HflC family / Band 7 domain / SPFH domain / Band 7 family / prohibitin homologues / Band 7/SPFH domain superfamily / Nucleic acid-binding, OB-fold
Similarity search - Domain/homology
Protein QmcA / Inner membrane protein YbbJ
Similarity search - Component
Biological speciesEscherichia coli (E. coli) / Escherichia coli (strain K12) (bacteria)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.9 Å
AuthorsQiao Z / Gao YG
Funding support Singapore, 1 items
OrganizationGrant numberCountry
Ministry of Education (MoE, Singapore) Singapore
CitationJournal: Structure / Year: 2024
Title: Cryo-EM structure of the SPFH-NfeD family protein complex QmcA-YbbJ.
Authors: Kwan Ann Tan / Zhu Qiao / Zachary Ze En Lim / Joshua Yi Yeo / Yonlada Yong / Phong Hoa Do / Ero Rya / Yong-Gui Gao /
Abstract: The SPFH (stomatin, prohibitin, flotillin, and HflK/C) protein family is universally present and encompasses the evolutionarily conserved SPFH domain. These proteins are predominantly localized in ...The SPFH (stomatin, prohibitin, flotillin, and HflK/C) protein family is universally present and encompasses the evolutionarily conserved SPFH domain. These proteins are predominantly localized in lipid raft and implicated in various biological processes. The NfeD (nodulation formation efficiency D) protein family is often encoded in tandem with SPFH proteins, suggesting a close functional relationship. Here, we elucidate the cryoelectron microscopy (cryo-EM) structure of the Escherichia coli QmcA-YbbJ complex belonging to the SPFH and NfeD families, respectively. Our findings reveal that the QmcA-YbbJ complex forms an intricate cage-like structure composed of 26 copies of QmcA-YbbJ heterodimers. The transmembrane helices of YbbJ act as adhesive elements bridging adjacent QmcA molecules, while the oligosaccharide-binding domain of YbbJ encapsulates the SPFH domain of QmcA. Our structural study significantly contributes to understanding the functional role of the NfeD protein family and sheds light on the interplay between SPFH and NfeD family proteins.
History
DepositionApr 18, 2024-
Header (metadata) releaseAug 21, 2024-
Map releaseAug 21, 2024-
UpdateOct 23, 2024-
Current statusOct 23, 2024Processing site: PDBj / Status: Released

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Structure visualization

Supplemental images

emd_39773.png

Downloads & links

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Map

FileDownload / File: emd_39773.map.gz / Format: CCP4 / Size: 64 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
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AxesZ (Sec.)Y (Row.)X (Col.)
1.46 Å/pix.
x 256 pix.
= 373.76 Å		1.46 Å/pix.
x 256 pix.
= 373.76 Å		1.46 Å/pix.
x 256 pix.
= 373.76 Å

Surface

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Images are generated by Spider.

Voxel sizeX=Y=Z: 1.46 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.08
Minimum - Maximum-0.0018179584 - 1.9883393
Average (Standard dev.)0.0038183292 (±0.043962277)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions256256256
Spacing256256256
CellA=B=C: 373.76 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: #2

Fileemd_39773_half_map_1.map
Projections & Slices
AxesZYX

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Slices (1/2)
Density Histograms

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Half map: #1

Fileemd_39773_half_map_2.map
Projections & Slices
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Sample components

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Entire : QmcA-YbbJ complex

EntireName: QmcA-YbbJ complex
Components
  • Complex: QmcA-YbbJ complex
    • Protein or peptide: Protein QmcA
    • Protein or peptide: Inner membrane protein YbbJ

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Supramolecule #1: QmcA-YbbJ complex

SupramoleculeName: QmcA-YbbJ complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Escherichia coli (E. coli)

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Macromolecule #1: Protein QmcA

MacromoleculeName: Protein QmcA / type: protein_or_peptide / ID: 1 / Number of copies: 26 / Enantiomer: LEVO
Source (natural)Organism: Escherichia coli (strain K12) (bacteria)
Molecular weightTheoretical: 33.778023 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MLIFIPILIF VALVIVGAGV KIVPQGYQWT VERFGRYTKT LQPGLSLVVP FMDRIGRKIN MMEQVLDIPS QEVISKDNAN VTIDAVCFI QVIDAPRAAY EVSNLELAII NLTMTNIRTV LGSMELDEML SQRDSINSRL LRIVDEATNP WGIKVTRIEI R DVRPPAEL ...String:
MLIFIPILIF VALVIVGAGV KIVPQGYQWT VERFGRYTKT LQPGLSLVVP FMDRIGRKIN MMEQVLDIPS QEVISKDNAN VTIDAVCFI QVIDAPRAAY EVSNLELAII NLTMTNIRTV LGSMELDEML SQRDSINSRL LRIVDEATNP WGIKVTRIEI R DVRPPAEL ISSMNAQMKA ERTKRAYILE AEGIRQAEIL KAEGEKQSQI LKAEGERQSA FLQAEARERS AEAEARATKM VS EAIASGD IQAVNYFVAQ KYTEALQQIG SSSNSKVVMM PLEASSLMGS IAGIAELVKD SANKRTQP

UniProtKB: Protein QmcA

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Macromolecule #2: Inner membrane protein YbbJ

MacromoleculeName: Inner membrane protein YbbJ / type: protein_or_peptide / ID: 2 / Number of copies: 26 / Enantiomer: LEVO
Source (natural)Organism: Escherichia coli (strain K12) (bacteria) / Strain: K12
Molecular weightTheoretical: 16.956775 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
MMELMVVHPH IFWLSLGGLL LAAEMLGGNG YLLWSGVAAV ITGLVVWLVP LGWEWQGVMF AILTLLAAWL WWKWLSRRVR EQKHSDSHL NQRGQQLIGR RFVLESPLVN GRGHMRVGDS SWPVSASEDL GAGTHVEVIA IEGITLHIRA VSS

UniProtKB: Inner membrane protein YbbJ

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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

Concentration5 mg/mL
BufferpH: 7.5
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: FEI FALCON IV (4k x 4k) / Average electron dose: 40.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 1.5 µm / Nominal defocus min: 0.5 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Startup modelType of model: OTHER
Final reconstructionResolution.type: BY AUTHOR / Resolution: 2.9 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 36372
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD

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