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- EMDB-22226: R. capsulatus cyt bc1 with both FeS proteins in b position (CIII2 b-b) -

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Basic information

Entry
Database: EMDB / ID: EMD-22226
TitleR. capsulatus cyt bc1 with both FeS proteins in b position (CIII2 b-b)
Map dataR. capsulatus cyt bc1 with both FeS proteins in b position (CIII2 b-b)
Sample
  • Complex: ubiquinol:cytochrome c reductase (complex III or cyt bc1 complex)
    • Protein or peptide: Cytochrome b
    • Protein or peptide: Cytochrome c1
    • Protein or peptide: Ubiquinol-cytochrome c reductase iron-sulfur subunit
  • Ligand: HEME C
  • Ligand: FE2/S2 (INORGANIC) CLUSTER
Function / homology
Function and homology information


respiratory chain complex III / quinol-cytochrome-c reductase / ubiquinol-cytochrome-c reductase activity / respirasome / respiratory electron transport chain / 2 iron, 2 sulfur cluster binding / electron transfer activity / intracellular membrane-bounded organelle / heme binding / metal ion binding ...respiratory chain complex III / quinol-cytochrome-c reductase / ubiquinol-cytochrome-c reductase activity / respirasome / respiratory electron transport chain / 2 iron, 2 sulfur cluster binding / electron transfer activity / intracellular membrane-bounded organelle / heme binding / metal ion binding / plasma membrane / cytoplasm
Similarity search - Function
Ubiquitinol-cytochrome C reductase, Fe-S subunit, TAT signal / Ubiquitinol-cytochrome C reductase Fe-S subunit TAT signal / Cytochrome b / : / : / Ubiquinol-cytochrome c reductase, iron-sulphur subunit / Cytochrome c1 / Cytochrome C1 family / Cytochrome b/b6, C-terminal / Cytochrome b(C-terminal)/b6/petD ...Ubiquitinol-cytochrome C reductase, Fe-S subunit, TAT signal / Ubiquitinol-cytochrome C reductase Fe-S subunit TAT signal / Cytochrome b / : / : / Ubiquinol-cytochrome c reductase, iron-sulphur subunit / Cytochrome c1 / Cytochrome C1 family / Cytochrome b/b6, C-terminal / Cytochrome b(C-terminal)/b6/petD / Cytochrome b/b6 C-terminal region profile. / Cytochrome b/b6, C-terminal domain superfamily / Cytochrome b/b6/petB / Twin-arginine translocation pathway, signal sequence, bacterial/archaeal / Rieske iron-sulphur protein, C-terminal / Cytochrome b/b6, N-terminal / Cytochrome b/b6-like domain superfamily / Cytochrome b/b6 N-terminal region profile. / Di-haem cytochrome, transmembrane / Rieske iron-sulphur protein / Rieske [2Fe-2S] iron-sulphur domain / Rieske [2Fe-2S] domain / Rieske [2Fe-2S] iron-sulfur domain profile. / Rieske [2Fe-2S] iron-sulphur domain superfamily / Cytochrome c family profile. / Cytochrome c-like domain / Cytochrome c-like domain superfamily / Twin arginine translocation (Tat) signal profile. / Twin-arginine translocation pathway, signal sequence
Similarity search - Domain/homology
Ubiquinol-cytochrome c reductase iron-sulfur subunit / Cytochrome b / Cytochrome c1
Similarity search - Component
Biological speciesRhodobacter capsulatus SB 1003 (bacteria) / Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003) (bacteria)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.5 Å
AuthorsSteimle S / Van Eeuwen T / Ozturk Y / Kim HJ / Braitbard M / Selamoglu N / Garcia BA / Schneidman-Duhovny D / Murakami K / Daldal F
Funding support United States, Israel, 8 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)R01-GM38237 United States
Department of Energy (DOE, United States)DE-FG02-91ER20052 United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)R01-GM123233 United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)T32-GM008275 United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)S10OD023592 United States
Israel Science Foundation1466/18 Israel
United States - Israel Binational Science Foundation (BSF)2016070 Israel
Israel Ministry of Science and Technology80802 Israel
CitationJournal: Nat Commun / Year: 2021
Title: Cryo-EM structures of engineered active bc-cbb type CIIICIV super-complexes and electronic communication between the complexes.
Authors: Stefan Steimle / Trevor van Eeuwen / Yavuz Ozturk / Hee Jong Kim / Merav Braitbard / Nur Selamoglu / Benjamin A Garcia / Dina Schneidman-Duhovny / Kenji Murakami / Fevzi Daldal /
Abstract: Respiratory electron transport complexes are organized as individual entities or combined as large supercomplexes (SC). Gram-negative bacteria deploy a mitochondrial-like cytochrome (cyt) bc (Complex ...Respiratory electron transport complexes are organized as individual entities or combined as large supercomplexes (SC). Gram-negative bacteria deploy a mitochondrial-like cytochrome (cyt) bc (Complex III, CIII), and may have specific cbb-type cyt c oxidases (Complex IV, CIV) instead of the canonical aa-type CIV. Electron transfer between these complexes is mediated by soluble (c) and membrane-anchored (c) cyts. Here, we report the structure of an engineered bc-cbb type SC (CIIICIV, 5.2 Å resolution) and three conformers of native CIII (3.3 Å resolution). The SC is active in vivo and in vitro, contains all catalytic subunits and cofactors, and two extra transmembrane helices attributed to cyt c and the assembly factor CcoH. The cyt c is integral to SC, its cyt domain is mobile and it conveys electrons to CIV differently than cyt c. The successful production of a native-like functional SC and determination of its structure illustrate the characteristics of membrane-confined and membrane-external respiratory electron transport pathways in Gram-negative bacteria.
History
DepositionJun 27, 2020-
Header (metadata) releaseDec 30, 2020-
Map releaseDec 30, 2020-
UpdateJul 14, 2021-
Current statusJul 14, 2021Processing site: RCSB / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.048
  • Imaged by UCSF Chimera
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  • Surface view colored by cylindrical radius
  • Surface level: 0.048
  • Imaged by UCSF Chimera
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  • Surface view with fitted model
  • Atomic models: PDB-6xkv
  • Surface level: 0.048
  • Imaged by UCSF Chimera
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_22226.png

Downloads & links

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Map

FileDownload / File: emd_22226.map.gz / Format: CCP4 / Size: 52.7 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationR. capsulatus cyt bc1 with both FeS proteins in b position (CIII2 b-b)
Voxel sizeX=Y=Z: 1.36 Å
Density
Contour LevelBy AUTHOR: 0.048 / Movie #1: 0.048
Minimum - Maximum-0.1615175 - 0.2435529
Average (Standard dev.)0.00018402674 (±0.004320249)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions240240240
Spacing240240240
CellA=B=C: 326.4 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.361.361.36
M x/y/z240240240
origin x/y/z0.0000.0000.000
length x/y/z326.400326.400326.400
α/β/γ90.00090.00090.000
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS240240240
D min/max/mean-0.1620.2440.000

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Supplemental data

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Sample components

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Entire : ubiquinol:cytochrome c reductase (complex III or cyt bc1 complex)

EntireName: ubiquinol:cytochrome c reductase (complex III or cyt bc1 complex)
Components
  • Complex: ubiquinol:cytochrome c reductase (complex III or cyt bc1 complex)
    • Protein or peptide: Cytochrome b
    • Protein or peptide: Cytochrome c1
    • Protein or peptide: Ubiquinol-cytochrome c reductase iron-sulfur subunit
  • Ligand: HEME C
  • Ligand: FE2/S2 (INORGANIC) CLUSTER

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Supramolecule #1: ubiquinol:cytochrome c reductase (complex III or cyt bc1 complex)

SupramoleculeName: ubiquinol:cytochrome c reductase (complex III or cyt bc1 complex)
type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#3
Source (natural)Organism: Rhodobacter capsulatus SB 1003 (bacteria)
Recombinant expressionOrganism: Rhodobacter capsulatus SB 1003 (bacteria) / Recombinant strain: YO12 / Recombinant plasmid: pYO76
Molecular weightTheoretical: 250 KDa

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Macromolecule #1: Cytochrome b

MacromoleculeName: Cytochrome b / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003) (bacteria)
Strain: ATCC BAA-309 / NBRC 16581 / SB1003
Molecular weightTheoretical: 49.386469 KDa
Recombinant expressionOrganism: Rhodobacter capsulatus SB 1003 (bacteria)
SequenceString: MSGIPHDHYE PKTGIEKWLH DRLPIVGLVY DTIMIPTPKN LNWWWIWGIV LAFTLVLQIV TGIVLAMHYT PHVDLAFASV EHIMRDVNG GWAMRYIHAN GASLFFLAVY IHIFRGLYYG SYKAPREITW IVGMVIYLLM MGTAFMGYVL PWGQMSFWGA T VITGLFGA ...String:
MSGIPHDHYE PKTGIEKWLH DRLPIVGLVY DTIMIPTPKN LNWWWIWGIV LAFTLVLQIV TGIVLAMHYT PHVDLAFASV EHIMRDVNG GWAMRYIHAN GASLFFLAVY IHIFRGLYYG SYKAPREITW IVGMVIYLLM MGTAFMGYVL PWGQMSFWGA T VITGLFGA IPGIGPSIQA WLLGGPAVDN ATLNRFFSLH YLLPFVIAAL VAIHIWAFHT TGNNNPTGVE VRRTSKADAE KD TLPFWPY FVIKDLFALA LVLLGFFAVV AYMPNYLGHP DNYVQANPLS TPAHIVPEWY FLPFYAILRA FAADVWVVIL VDG LTFGIV DAKFFGVIAM FGAIAVMALA PWLDTSKVRS GAYRPKFRMW FWFLVLDFVV LTWVGAMPTE YPYDWISLIA STYW FAYFL VILPLLGATE KPEPIPASIE EDFNSHYGNP AE

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Macromolecule #2: Cytochrome c1

MacromoleculeName: Cytochrome c1 / type: protein_or_peptide / ID: 2 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003) (bacteria)
Strain: ATCC BAA-309 / NBRC 16581 / SB1003
Molecular weightTheoretical: 30.352615 KDa
Recombinant expressionOrganism: Rhodobacter capsulatus SB 1003 (bacteria)
SequenceString: MKKLLISAVS ALVLGSGAAF ANSNVPDHAF SFEGIFGKYD QAQLRRGFQV YNEVCSACHG MKFVPIRTLA DDGGPQLDPT FVREYAAGL DTIIDKDSGE ERDRKETDMF PTRVGDGMGP DLSVMAKARA GFSGPAGSGM NQLFKGMGGP EYIYNYVIGF E ENPECAPE ...String:
MKKLLISAVS ALVLGSGAAF ANSNVPDHAF SFEGIFGKYD QAQLRRGFQV YNEVCSACHG MKFVPIRTLA DDGGPQLDPT FVREYAAGL DTIIDKDSGE ERDRKETDMF PTRVGDGMGP DLSVMAKARA GFSGPAGSGM NQLFKGMGGP EYIYNYVIGF E ENPECAPE GIDGYYYNKT FQIGGVPDTC KDAAGVKITH GSWARMPPPL VDDQVTYEDG TPATVDQMAQ DVSAFLMWAA EP KLVARKQ MGLVAMVMLG LLSVMLYLTN KRLWAPYKGH KA

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Macromolecule #3: Ubiquinol-cytochrome c reductase iron-sulfur subunit

MacromoleculeName: Ubiquinol-cytochrome c reductase iron-sulfur subunit / type: protein_or_peptide / ID: 3 / Number of copies: 2 / Enantiomer: LEVO / EC number: quinol-cytochrome-c reductase
Source (natural)Organism: Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003) (bacteria)
Strain: ATCC BAA-309 / NBRC 16581 / SB1003
Molecular weightTheoretical: 20.465109 KDa
Recombinant expressionOrganism: Rhodobacter capsulatus SB 1003 (bacteria)
SequenceString:
MSHAEDNAGT RRDFLYHATA ATGVVVTGAA VWPLINQMNA SADVKAMASI FVDVSAVEVG TQLTVKWRGK PVFIRRRDEK DIELARSVP LGALRDTSAE NANKPGAEAT DENRTLPAFD GTNTGEWLVM LGVCTHLGCV PMGDKSGDFG GWFCPCHGSH Y DSAGRIRK GPAPRNLDIP VAAFVDETTI KLG

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Macromolecule #4: HEME C

MacromoleculeName: HEME C / type: ligand / ID: 4 / Number of copies: 6 / Formula: HEC
Molecular weightTheoretical: 618.503 Da
Chemical component information

ChemComp-HEC:
HEME C / Heme C

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Macromolecule #5: FE2/S2 (INORGANIC) CLUSTER

MacromoleculeName: FE2/S2 (INORGANIC) CLUSTER / type: ligand / ID: 5 / Number of copies: 2 / Formula: FES
Molecular weightTheoretical: 175.82 Da
Chemical component information

ChemComp-FES:
FE2/S2 (INORGANIC) CLUSTER / Iron–sulfur cluster

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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

Concentration4 mg/mL
BufferpH: 7.4
GridModel: C-flat-1.2/1.3 / Material: COPPER / Mesh: 400 / Pretreatment - Type: GLOW DISCHARGE
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 298 K / Instrument: FEI VITROBOT MARK IV

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: SPOT SCAN / Imaging mode: BRIGHT FIELDBright-field microscopy
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 40.0 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Particle selectionNumber selected: 733210
CTF correctionSoftware - Name: RELION (ver. 3.0) / Software - details: CTFFIND 4.1 was used
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION (ver. 3.0)
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION (ver. 3.0)
Final reconstructionApplied symmetry - Point group: C2 (2 fold cyclic) / Resolution.type: BY AUTHOR / Resolution: 3.5 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 3.0) / Number images used: 37710
FSC plot (resolution estimation)

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Atomic model buiding 1

Initial modelPDB ID:

6xi0

RefinementSpace: REAL / Protocol: RIGID BODY FIT / Overall B value: 54 / Target criteria: Correlation coefficient
Output model

PDB-6xkv:
R. capsulatus cyt bc1 with both FeS proteins in b position (CIII2 b-b)

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