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Open data
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Basic information
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Title | Bcs1 bound with ISP-ED | |||||||||
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![]() | Heptamer / TRANSLOCASE / AAA-ATPase / substrate-bound | |||||||||
Function / homology | ![]() mitochondrial protein-transporting ATPase activity / protein insertion into mitochondrial inner membrane from matrix / mitochondrial cytochrome c oxidase assembly / mitochondrial respiratory chain complex III assembly / Respiratory electron transport / : / quinol-cytochrome-c reductase / ubiquinol-cytochrome-c reductase activity / mitochondrial electron transport, ubiquinol to cytochrome c / mitochondrial respiratory chain complex I assembly ...mitochondrial protein-transporting ATPase activity / protein insertion into mitochondrial inner membrane from matrix / mitochondrial cytochrome c oxidase assembly / mitochondrial respiratory chain complex III assembly / Respiratory electron transport / : / quinol-cytochrome-c reductase / ubiquinol-cytochrome-c reductase activity / mitochondrial electron transport, ubiquinol to cytochrome c / mitochondrial respiratory chain complex I assembly / 2 iron, 2 sulfur cluster binding / mitochondrial inner membrane / oxidoreductase activity / ATP hydrolysis activity / mitochondrion / ATP binding / metal ion binding / plasma membrane Similarity search - Function | |||||||||
Biological species | ![]() ![]() ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 7.2 Å | |||||||||
![]() | Zhan J / Xia D | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Conformations of Bcs1L undergoing ATP hydrolysis suggest a concerted translocation mechanism for folded iron-sulfur protein substrate. Authors: Jingyu Zhan / Allison Zeher / Rick Huang / Wai Kwan Tang / Lisa M Jenkins / Di Xia / ![]() Abstract: The human AAA-ATPase Bcs1L translocates the fully assembled Rieske iron-sulfur protein (ISP) precursor across the mitochondrial inner membrane, enabling respiratory Complex III assembly. Exactly how ...The human AAA-ATPase Bcs1L translocates the fully assembled Rieske iron-sulfur protein (ISP) precursor across the mitochondrial inner membrane, enabling respiratory Complex III assembly. Exactly how the folded substrate is bound to and released from Bcs1L has been unclear, and there has been ongoing debate as to whether subunits of Bcs1L act in sequence or in unison hydrolyzing ATP when moving the protein cargo. Here, we captured Bcs1L conformations by cryo-EM during active ATP hydrolysis in the presence or absence of ISP substrate. In contrast to the threading mechanism widely employed by AAA proteins in substrate translocation, subunits of Bcs1L alternate uniformly between ATP and ADP conformations without detectable intermediates that have different, co-existing nucleotide states, indicating that the subunits act in concert. We further show that the ISP can be trapped by Bcs1 when its subunits are all in the ADP-bound state, which we propose to be released in the apo form. | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 87 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 15.5 KB 15.5 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 12.1 KB | Display | ![]() |
Images | ![]() | 81 KB | ||
Filedesc metadata | ![]() | 5.2 KB | ||
Others | ![]() ![]() | 165.3 MB 165.3 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 1.2 MB | Display | ![]() |
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Full document | ![]() | 1.2 MB | Display | |
Data in XML | ![]() | 20.3 KB | Display | |
Data in CIF | ![]() | 25.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8t14C ![]() 8t5uC ![]() 8t7uC ![]() 8tbyC ![]() 8ti0C ![]() 8tp1C ![]() 8tplC C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
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Voxel size | X=Y=Z: 0.83 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #2
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_41609_half_map_2.map | ||||||||||||
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Density Histograms |
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Sample components
-Entire : Bcs1 bound with ISP-ED
Entire | Name: Bcs1 bound with ISP-ED |
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Components |
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-Supramolecule #1: Bcs1 bound with ISP-ED
Supramolecule | Name: Bcs1 bound with ISP-ED / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Molecular weight | Theoretical: 340 KDa |
-Supramolecule #2: A WATER SOLUBLE FRAGMENT OF THE RIESKE IRON-SULFUR PROTEIN OF THE...
Supramolecule | Name: A WATER SOLUBLE FRAGMENT OF THE RIESKE IRON-SULFUR PROTEIN OF THE BOVINE HEART MITOCHONDRIAL CYTOCHROME BC1-COMPLEX type: complex / ID: 2 / Parent: 1 / Macromolecule list: #2 |
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Source (natural) | Organism: ![]() ![]() |
-Supramolecule #3: Mitochondrial chaperone BCS1
Supramolecule | Name: Mitochondrial chaperone BCS1 / type: complex / ID: 3 / Parent: 1 / Macromolecule list: #1 |
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Source (natural) | Organism: ![]() ![]() |
-Macromolecule #1: Mitochondrial chaperone BCS1
Macromolecule | Name: Mitochondrial chaperone BCS1 / type: protein_or_peptide / ID: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Recombinant expression | Organism: ![]() |
Sequence | String: MPFSDFVLAL KDNPYFGAGF GLVGVGTALA MARKGAQLGL VAFRRHYMIT LEVPARDRSY AWLLSWLTRH STRTQHLSVE TSYLQHESGR ISTKFEFIPS PGNHFIWYQG KWIRVERNRD MQMVDLQTGT PWESVTFTAL GTDRKVFFNI LEEARALALQ QEEGKTVMYT ...String: MPFSDFVLAL KDNPYFGAGF GLVGVGTALA MARKGAQLGL VAFRRHYMIT LEVPARDRSY AWLLSWLTRH STRTQHLSVE TSYLQHESGR ISTKFEFIPS PGNHFIWYQG KWIRVERNRD MQMVDLQTGT PWESVTFTAL GTDRKVFFNI LEEARALALQ QEEGKTVMYT AVGSEWRTFG YPRRRRPLDS VVLQQGLADR IVKDIREFID NPKWYIDRGI PYRRGYLLYG PPGCGKSSFI TALAGELEHS ICLLSLTDSS LSDDRLNHLL SVAPQQSLVL LEDVDAAFLS RDLAVENPIK YQGLGRLTFS GLLNALDGVA STEARIVFMT TNYIDRLDPA LIRPGRVDLK EYVGYCSHWQ LTQMFQRFYP GQAPSLAENF AEHVLKATSE ISPAQVQGYF MLYKNDPMGA VHNIESLRHH HHHH UniProtKB: Mitochondrial chaperone BCS1 |
-Macromolecule #2: RIESKE IRON-SULFUR PROTEIN
Macromolecule | Name: RIESKE IRON-SULFUR PROTEIN / type: protein_or_peptide / ID: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Sequence | String: VLAMSKIEIK LSDIPEGKNM AFKWRGKPLF VRHRTKKEID QEAAVEVSQL RDPQHDLERV KKPEWVILIG VCTHLGCVPI ANAGDFGGYY CPCHGSHYDA SGRIRKGPAP LNLEVPSYEF TSDDMVIVG UniProtKB: Cytochrome b-c1 complex subunit Rieske, mitochondrial |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 8 |
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Grid | Model: UltrAuFoil / Material: GOLD |
Vitrification | Cryogen name: ETHANE / Chamber humidity: 95 % / Chamber temperature: 277.15 K |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Number grids imaged: 1 / Average electron dose: 54.4 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.0 µm / Nominal defocus min: 0.7000000000000001 µm |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |