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- EMDB-20808: Apo mBcs1 -

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Basic information

Entry
Database: EMDB / ID: EMD-20808
TitleApo mBcs1
Map dataApo mbcs1
Sample
  • Complex: Apo structure of mBcs1 heptamer
    • Protein or peptide: Mitochondrial chaperone BCS1
Keywordsbcs1 / AAA ATPases / mitochondrial inner membrane / CHAPERONE
Function / homology
Function and homology information


mitochondrial protein-transporting ATPase activity / protein insertion into mitochondrial inner membrane from matrix / mitochondrial cytochrome c oxidase assembly / mitochondrial respiratory chain complex III assembly / mitochondrial respiratory chain complex I assembly / mitochondrial inner membrane / ATP hydrolysis activity / mitochondrion / ATP binding
Similarity search - Function
BCS1, N-terminal / BCS1 N terminal / BCS1_N / ATPase, AAA-type, conserved site / AAA-protein family signature. / ATPase family associated with various cellular activities (AAA) / ATPase, AAA-type, core / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
Mitochondrial chaperone BCS1
Similarity search - Component
Biological speciesMus musculus (house mouse)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.81 Å
AuthorsTang WK / Borgnia MJ
Funding support United States, 1 items
OrganizationGrant numberCountry
National Institutes of Health/National Cancer Institute (NIH/NCI) United States
CitationJournal: Nat Struct Mol Biol / Year: 2020
Title: Structures of AAA protein translocase Bcs1 suggest translocation mechanism of a folded protein.
Authors: Wai Kwan Tang / Mario J Borgnia / Allen L Hsu / Lothar Esser / Tara Fox / Natalia de Val / Di Xia /
Abstract: The mitochondrial membrane-bound AAA protein Bcs1 translocate substrates across the mitochondrial inner membrane without previous unfolding. One substrate of Bcs1 is the iron-sulfur protein (ISP), a ...The mitochondrial membrane-bound AAA protein Bcs1 translocate substrates across the mitochondrial inner membrane without previous unfolding. One substrate of Bcs1 is the iron-sulfur protein (ISP), a subunit of the respiratory Complex III. How Bcs1 translocates ISP across the membrane is unknown. Here we report structures of mouse Bcs1 in two different conformations, representing three nucleotide states. The apo and ADP-bound structures reveal a homo-heptamer and show a large putative substrate-binding cavity accessible to the matrix space. ATP binding drives a contraction of the cavity by concerted motion of the ATPase domains, which could push substrate across the membrane. Our findings shed light on the potential mechanism of translocating folded proteins across a membrane, offer insights into the assembly process of Complex III and allow mapping of human disease-associated mutations onto the Bcs1 structure.
History
DepositionOct 5, 2019-
Header (metadata) releaseNov 27, 2019-
Map releaseFeb 12, 2020-
UpdateMar 20, 2024-
Current statusMar 20, 2024Processing site: RCSB / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.016
  • Imaged by UCSF Chimera
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  • Surface view colored by cylindrical radius
  • Surface level: 0.016
  • Imaged by UCSF Chimera
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  • Surface view with fitted model
  • Atomic models: PDB-6ukp
  • Surface level: 0.03
  • Imaged by UCSF Chimera
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  • Simplified surface model + fitted atomic model
  • Atomic modelsPDB-6ukp
  • Imaged by Jmol
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_20808.png

Downloads & links

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Map

FileDownload / File: emd_20808.map.gz / Format: CCP4 / Size: 23.8 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationApo mbcs1
Voxel sizeX=Y=Z: 1.72 Å
Density
Contour LevelBy AUTHOR: 0.016 / Movie #1: 0.016
Minimum - Maximum-0.0063258875 - 0.5929009
Average (Standard dev.)0.00027760395 (±0.009313316)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions184184184
Spacing184184184
CellA=B=C: 316.48 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.721.721.72
M x/y/z184184184
origin x/y/z0.0000.0000.000
length x/y/z316.480316.480316.480
α/β/γ90.00090.00090.000
start NX/NY/NZ-38-19-20
NX/NY/NZ858082
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS184184184
D min/max/mean-0.0060.5930.000

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Supplemental data

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Sample components

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Entire : Apo structure of mBcs1 heptamer

EntireName: Apo structure of mBcs1 heptamer
Components
  • Complex: Apo structure of mBcs1 heptamer
    • Protein or peptide: Mitochondrial chaperone BCS1

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Supramolecule #1: Apo structure of mBcs1 heptamer

SupramoleculeName: Apo structure of mBcs1 heptamer / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Mus musculus (house mouse)

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Macromolecule #1: Mitochondrial chaperone BCS1

MacromoleculeName: Mitochondrial chaperone BCS1 / type: protein_or_peptide / ID: 1 / Number of copies: 7 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 48.659281 KDa
Recombinant expressionOrganism: Komagataella pastoris (fungus)
SequenceString: MPFSDFVLAL KDNPYFGAGF GLVGVGTALA MARKGAQLGL VAFRRHYMIT LEVPARDRSY AWLLSWLTRH STRTQHLSVE TSYLQHESG RISTKFEFIP SPGNHFIWYQ GKWIRVERNR DMQMVDLQTG TPWESVTFTA LGTDRKVFFN ILEEARALAL Q QEEGKTVM ...String:
MPFSDFVLAL KDNPYFGAGF GLVGVGTALA MARKGAQLGL VAFRRHYMIT LEVPARDRSY AWLLSWLTRH STRTQHLSVE TSYLQHESG RISTKFEFIP SPGNHFIWYQ GKWIRVERNR DMQMVDLQTG TPWESVTFTA LGTDRKVFFN ILEEARALAL Q QEEGKTVM YTAVGSEWRT FGYPRRRRPL DSVVLQQGLA DRIVKDIREF IDNPKWYIDR GIPYRRGYLL YGPPGCGKSS FI TALAGEL EHSICLLSLT DSSLSDDRLN HLLSVAPQQS LVLLEDVDAA FLSRDLAVEN PIKYQGLGRL TFSGLLNALD GVA STEARI VFMTTNYIDR LDPALIRPGR VDLKEYVGYC SHWQLTQMFQ RFYPGQAPSL AENFAEHVLK ATSEISPAQV QGYF MLYKN DPMGAVHNIE SLRPRDHHHH HH

UniProtKB: Mitochondrial chaperone BCS1

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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: 8.5
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K2 SUMMIT (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
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Startup modelType of model: NONE
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.81 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 67261
Initial angle assignmentType: NOT APPLICABLE
Final angle assignmentType: NOT APPLICABLE

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