Cryo-EM structure of Euglena gracilis super-complex I+III2+IV, composite
Components
(Cytochrome c oxidase subunit ...) x 2
(NDUEG11) x 2
(Ubiquinol-cytochrome- ...) x 2
COX4
COX5b-2
COX5c
COX6a
COX6b-1
COX7a
COX7c
COXEG1
COXEG10
COXEG3
COXEG4
COXEG5
COXEG6
COXEG7
COXEG8
COXEG9
Cytochrome b
Cytochrome c1, heme protein
MPP-beta
NADH-ubiquinone oxidoreductase chain 4
ND1
ND2a
ND2b
ND3
ND4L
ND5
NDUCA1
NDUCA2
NDUCA3
NDUEG1
NDUEG10
NDUEG13
NDUEG2
NDUEG3
NDUEG4
NDUEG5
NDUEG6
NDUEG7
NDUEG8
NDUEG9
NDUFA1
NDUFA11
NDUFA12
NDUFA13
NDUFA2
NDUFA3
NDUFA5
NDUFA6
NDUFA7
NDUFA8
NDUFA9
NDUFAB1-alpha
NDUFAB1-beta
NDUFB10
NDUFB11
NDUFB2
NDUFB3
NDUFB4
NDUFB5
NDUFB6
NDUFB7
NDUFB8
NDUFB9
NDUFC2
NDUFS1a
NDUFS1b
NDUFS2
NDUFS3
NDUFS4
NDUFS5
NDUFS6
NDUFS7
NDUFS8
NDUFV1
NDUFV2
NDUFX
Putative NADH dehydrogenase subunit 6
UQCR10
UQCR9
UQCRB
UQCRFS1
UQCRH
UQCRQ
poly(UNK)
Keywords
ELECTRON TRANSPORT / Electron transport chain / supercomplex / membrane protein / Euglena gracilis
Function / homology
Function and homology information
: / : / cytochrome-c oxidase / quinol-cytochrome-c reductase / ubiquinol-cytochrome-c reductase activity / mitochondrial electron transport, cytochrome c to oxygen / cytochrome-c oxidase activity / mitochondrial electron transport, ubiquinol to cytochrome c / NADH:ubiquinone reductase (H+-translocating) / electron transport coupled proton transport ...: / : / cytochrome-c oxidase / quinol-cytochrome-c reductase / ubiquinol-cytochrome-c reductase activity / mitochondrial electron transport, cytochrome c to oxygen / cytochrome-c oxidase activity / mitochondrial electron transport, ubiquinol to cytochrome c / NADH:ubiquinone reductase (H+-translocating) / electron transport coupled proton transport / NADH dehydrogenase (ubiquinone) activity / ATP synthesis coupled electron transport / : / respiratory electron transport chain / mitochondrial membrane / electron transport chain / mitochondrial inner membrane / electron transfer activity / oxidoreductase activity / copper ion binding / heme binding / mitochondrion / membrane / metal ion binding Similarity search - Function
Cytochrome C oxidase subunit II, transmembrane domain / Cytochrome C oxidase subunit II, transmembrane domain / Cytochrome oxidase subunit II transmembrane region profile. / Cytochrome c oxidase subunit III-like superfamily / Cytochrome c1, transmembrane anchor, C-terminal / Cytochrome c/quinol oxidase subunit II / : / Cytochrome c1 / Cytochrome C1 family / Copper centre Cu(A) ...Cytochrome C oxidase subunit II, transmembrane domain / Cytochrome C oxidase subunit II, transmembrane domain / Cytochrome oxidase subunit II transmembrane region profile. / Cytochrome c oxidase subunit III-like superfamily / Cytochrome c1, transmembrane anchor, C-terminal / Cytochrome c/quinol oxidase subunit II / : / Cytochrome c1 / Cytochrome C1 family / Copper centre Cu(A) / CO II and nitrous oxide reductase dinuclear copper centers signature. / Cytochrome C oxidase subunit II, transmembrane domain superfamily / 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 / Cytochrome c oxidase, subunit I, copper-binding site / Heme-copper oxidase catalytic subunit, copper B binding region signature. / Cytochrome c oxidase-like, subunit I domain / Cytochrome oxidase subunit I profile. / Cytochrome c oxidase subunit I / Cytochrome c oxidase-like, subunit I superfamily / Cytochrome C and Quinol oxidase polypeptide I / Cytochrome C oxidase subunit II, periplasmic domain / Cytochrome c oxidase subunit II-like C-terminal / Cytochrome oxidase subunit II copper A binding domain profile. / Cytochrome b/b6, N-terminal / Cytochrome b/b6-like domain superfamily / Cytochrome b/b6 N-terminal region profile. / Di-haem cytochrome, transmembrane / Peptidase M16, N-terminal / Insulinase (Peptidase family M16) / Metalloenzyme, LuxS/M16 peptidase-like / NADH:ubiquinone oxidoreductase / NADH:quinone oxidoreductase/Mrp antiporter, membrane subunit / Proton-conducting membrane transporter / Cytochrome c-like domain superfamily / Cupredoxin Similarity search - Domain/homology
1,2-Distearoyl-sn-glycerophosphoethanolamine / CARDIOLIPIN / COPPER (II) ION / FE2/S2 (INORGANIC) CLUSTER / FLAVIN MONONUCLEOTIDE / HEME-A / HEME C / PROTOPORPHYRIN IX CONTAINING FE / : / Chem-NDP ...1,2-Distearoyl-sn-glycerophosphoethanolamine / CARDIOLIPIN / COPPER (II) ION / FE2/S2 (INORGANIC) CLUSTER / FLAVIN MONONUCLEOTIDE / HEME-A / HEME C / PROTOPORPHYRIN IX CONTAINING FE / : / Chem-NDP / 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE / 1,2-DILAUROYL-SN-GLYCERO-3-PHOSPHATE / Chem-S12 / IRON/SULFUR CLUSTER / UBIQUINONE-10 / Chem-ZMP / Cytochrome b / NADH-ubiquinone oxidoreductase chain 4 / Cytochrome c1, heme protein / Ubiquinol-cytochrome-c reductase complex core protein 2, mitochondrial / Ubiquinol-cytochrome-C reductase complex subunit IX, mitochondrial / Cytochrome c oxidase subunit 1 / Putative NADH dehydrogenase subunit 6 / Cytochrome c oxidase subunit 2 Similarity search - Component
Biological species
Euglena gracilis (euglena)
Method
ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.81 Å
Journal: Nat Commun / Year: 2024 Title: Euglena's atypical respiratory chain adapts to the discoidal cristae and flexible metabolism. Authors: Zhaoxiang He / Mengchen Wu / Hongtao Tian / Liangdong Wang / Yiqi Hu / Fangzhu Han / Jiancang Zhou / Yong Wang / Long Zhou / Abstract: Euglena gracilis, a model organism of the eukaryotic supergroup Discoba harbouring also clinically important parasitic species, possesses diverse metabolic strategies and an atypical electron ...Euglena gracilis, a model organism of the eukaryotic supergroup Discoba harbouring also clinically important parasitic species, possesses diverse metabolic strategies and an atypical electron transport chain. While structures of the electron transport chain complexes and supercomplexes of most other eukaryotic clades have been reported, no similar structure is currently available for Discoba, limiting the understandings of its core metabolism and leaving a gap in the evolutionary tree of eukaryotic bioenergetics. Here, we report high-resolution cryo-EM structures of Euglena's respirasome I + III + IV and supercomplex III + IV. A previously unreported fatty acid synthesis domain locates on the tip of complex I's peripheral arm, providing a clear picture of its atypical subunit composition identified previously. Individual complexes are re-arranged in the respirasome to adapt to the non-uniform membrane curvature of the discoidal cristae. Furthermore, Euglena's conformationally rigid complex I is deactivated by restricting ubiquinone's access to its substrate tunnel. Our findings provide structural insights for therapeutic developments against euglenozoan parasite infections.
Average exposure time: 7.8 sec. / Electron dose: 51.5 e/Å2 / Film or detector model: FEI FALCON IV (4k x 4k) / Num. of grids imaged: 1 / Num. of real images: 9807
Image scans
Width: 4096 / Height: 4096
-
Processing
Software
Name
Version
Classification
phenix.real_space_refine
1.20.1_4487
refinement
PHENIX
1.20.1_4487
refinement
EM software
ID
Name
Version
Category
1
crYOLO
1.6.0
particleselection
2
EPU
imageacquisition
4
CTFFIND
4.1
CTFcorrection
7
PHENIX
1.20.1
modelfitting
8
Coot
0.9.6
modelfitting
10
cryoSPARC
v3.3.2
initialEulerassignment
11
cryoSPARC
v3.3.2
finalEulerassignment
12
cryoSPARC
v3.3.2
classification
13
v3.3.2
3Dreconstruction
14
PHENIX
1.20.1
modelrefinement
CTF correction
Type: PHASE FLIPPING AND AMPLITUDE CORRECTION
Particle selection
Num. of particles selected: 3232325
Symmetry
Point symmetry: C1 (asymmetric)
3D reconstruction
Resolution: 2.81 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 345048 / Algorithm: FOURIER SPACE / Num. of class averages: 1 / Symmetry type: POINT
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