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- PDB-6tml: Cryo-EM structure of Toxoplasma gondii mitochondrial ATP synthase... -

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Basic information

Entry
Database: PDB / ID: 6tml
TitleCryo-EM structure of Toxoplasma gondii mitochondrial ATP synthase hexamer, composite model
Components
  • (ATP synthase subunit ...) x 5
  • ATPTG1
  • ATPTG10
  • ATPTG11
  • ATPTG12
  • ATPTG13
  • ATPTG14
  • ATPTG15
  • ATPTG16
  • ATPTG17,ATPTG17,ATPTG17
  • ATPTG2
  • ATPTG3
  • ATPTG4
  • ATPTG5
  • ATPTG6
  • ATPTG7
  • ATPTG8
  • ATPTG9
  • Inhibitor of F1
  • Oligomycin sensitivity conferring protein (OSCP)
  • subunit 8
  • subunit a
  • subunit b
  • subunit c
  • subunit d
  • subunit f
  • subunit i/j
  • subunit k
KeywordsMEMBRANE PROTEIN / mitochondrial / ATP synthase / hexamer
Function / homology
Function and homology information


mitochondrial respiratory chain complex III / photosynthetic electron transport in photosystem I / mitochondrial proton-transporting ATP synthase, stator stalk / mitochondrial electron transport, ubiquinol to cytochrome c / mitochondrial proton-transporting ATP synthase, catalytic core / mitochondrial proton-transporting ATP synthase complex, coupling factor F(o) / mitochondrial proton-transporting ATP synthase complex, catalytic sector F(1) / mitochondrial proton-transporting ATP synthase complex / photosynthetic electron transport in photosystem II / proton motive force-driven ATP synthesis ...mitochondrial respiratory chain complex III / photosynthetic electron transport in photosystem I / mitochondrial proton-transporting ATP synthase, stator stalk / mitochondrial electron transport, ubiquinol to cytochrome c / mitochondrial proton-transporting ATP synthase, catalytic core / mitochondrial proton-transporting ATP synthase complex, coupling factor F(o) / mitochondrial proton-transporting ATP synthase complex, catalytic sector F(1) / mitochondrial proton-transporting ATP synthase complex / photosynthetic electron transport in photosystem II / proton motive force-driven ATP synthesis / proton transmembrane transporter activity / chloroplast thylakoid membrane / proton motive force-driven mitochondrial ATP synthesis / proton-transporting ATP synthase complex, catalytic core F(1) / H+-transporting two-sector ATPase / proton-transporting ATPase activity, rotational mechanism / proton-transporting ATP synthase activity, rotational mechanism / ADP binding / electron transfer activity / hydrolase activity / lipid binding / heme binding / ATP hydrolysis activity / ATP binding / membrane / metal ion binding / plasma membrane
Similarity search - Function
: / ATPTG10-like / Cytochrome c1, transmembrane anchor, C-terminal / Cytochrome c1 / Cytochrome C1 family / ATP synthase, F0 complex, subunit D superfamily, mitochondrial / ATP synthase, F1 complex, epsilon subunit, mitochondrial / ATP synthase, F1 complex, epsilon subunit superfamily, mitochondrial / Mitochondrial ATP synthase epsilon chain / Thioredoxin ...: / ATPTG10-like / Cytochrome c1, transmembrane anchor, C-terminal / Cytochrome c1 / Cytochrome C1 family / ATP synthase, F0 complex, subunit D superfamily, mitochondrial / ATP synthase, F1 complex, epsilon subunit, mitochondrial / ATP synthase, F1 complex, epsilon subunit superfamily, mitochondrial / Mitochondrial ATP synthase epsilon chain / Thioredoxin / F1F0 ATP synthase OSCP/delta subunit, N-terminal domain superfamily / ATPase, OSCP/delta subunit / ATP synthase delta (OSCP) subunit / ATP synthase, F1 complex, delta/epsilon subunit / ATP synthase, F1 complex, delta/epsilon subunit, N-terminal / F0F1 ATP synthase delta/epsilon subunit, N-terminal / ATP synthase, Delta/Epsilon chain, beta-sandwich domain / ATP synthase, F0 complex, subunit C / F1F0 ATP synthase subunit C superfamily / ATP synthase, F0 complex, subunit C, DCCD-binding site / ATP synthase c subunit signature. / ATP synthase, F1 complex, gamma subunit conserved site / ATP synthase gamma subunit signature. / ATP synthase, F1 complex, beta subunit / ATP synthase, alpha subunit, C-terminal domain superfamily / ATP synthase, F1 complex, gamma subunit / ATP synthase, F1 complex, gamma subunit superfamily / ATP synthase / ATP synthase, alpha subunit, C-terminal / ATP synthase, F1 complex, alpha subunit / ATP synthase, F1 complex, alpha subunit nucleotide-binding domain / ATP synthase alpha/beta chain, C terminal domain / V-ATPase proteolipid subunit C-like domain / F/V-ATP synthase subunit C superfamily / ATP synthase subunit C / ATPase, F1/V1 complex, beta/alpha subunit, C-terminal / ATP synthase subunit alpha, N-terminal domain-like superfamily / ATPase, F1/V1/A1 complex, alpha/beta subunit, N-terminal domain superfamily / Cytochrome c family profile. / Cytochrome c-like domain / ATPase, F1/V1/A1 complex, alpha/beta subunit, N-terminal domain / ATP synthase alpha/beta family, beta-barrel domain / ATPase, alpha/beta subunit, nucleotide-binding domain, active site / ATP synthase alpha and beta subunits signature. / Cytochrome c-like domain superfamily / ATPase, F1/V1/A1 complex, alpha/beta subunit, nucleotide-binding domain / ATP synthase alpha/beta family, nucleotide-binding domain / Thioredoxin domain / Thioredoxin-like superfamily / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
Uncharacterized protein / Putative ATP synthase F0 subunit 9 / Uncharacterized protein / ATP synthase F1, delta subunit protein / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7 / Uncharacterized protein / Putative membrane protein / Transmembrane protein / ATPTG10-like domain-containing protein / Transmembrane protein ...Uncharacterized protein / Putative ATP synthase F0 subunit 9 / Uncharacterized protein / ATP synthase F1, delta subunit protein / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7 / Uncharacterized protein / Putative membrane protein / Transmembrane protein / ATPTG10-like domain-containing protein / Transmembrane protein / Uncharacterized protein / Putative ATP synthase / Transmembrane protein / Transmembrane protein / Uncharacterized protein / ATP synthase subunit gamma, mitochondrial / CHCH domain-containing protein / Uncharacterized protein / ATP synthase subunit beta / Transmembrane protein / Transmembrane protein / ATP synthase subunit alpha / Thioredoxin domain-containing protein / Uncharacterized protein / Uncharacterized protein / Transmembrane protein / Putative atp synthase F1, epsilon subunit / Uncharacterized protein / Transmembrane protein / Putative myosin heavy chain / Cytochrome c1, heme protein / Uncharacterized protein
Similarity search - Component
Biological speciesToxoplasma gondii (eukaryote)
Toxoplasma gondii GT1 (eukaryote)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 4.8 Å
AuthorsMuhleip, A. / Kock Flygaard, R. / Amunts, A.
Funding support Sweden, 4items
OrganizationGrant numberCountry
Swedish Research CouncilNT_2015-04107 Sweden
European Research CouncilERC-2018-StG-805230 Sweden
Knut and Alice Wallenberg Foundation2018.0080 Sweden
European Molecular Biology OrganizationALTF 260-2017 Sweden
CitationJournal: Nat Commun / Year: 2021
Title: ATP synthase hexamer assemblies shape cristae of Toxoplasma mitochondria.
Authors: Alexander Mühleip / Rasmus Kock Flygaard / Jana Ovciarikova / Alice Lacombe / Paula Fernandes / Lilach Sheiner / Alexey Amunts /
Abstract: Mitochondrial ATP synthase plays a key role in inducing membrane curvature to establish cristae. In Apicomplexa causing diseases such as malaria and toxoplasmosis, an unusual cristae morphology has ...Mitochondrial ATP synthase plays a key role in inducing membrane curvature to establish cristae. In Apicomplexa causing diseases such as malaria and toxoplasmosis, an unusual cristae morphology has been observed, but its structural basis is unknown. Here, we report that the apicomplexan ATP synthase assembles into cyclic hexamers, essential to shape their distinct cristae. Cryo-EM was used to determine the structure of the hexamer, which is held together by interactions between parasite-specific subunits in the lumenal region. Overall, we identified 17 apicomplexan-specific subunits, and a minimal and nuclear-encoded subunit-a. The hexamer consists of three dimers with an extensive dimer interface that includes bound cardiolipins and the inhibitor IF. Cryo-ET and subtomogram averaging revealed that hexamers arrange into ~20-megadalton pentagonal pyramids in the curved apical membrane regions. Knockout of the linker protein ATPTG11 resulted in the loss of pentagonal pyramids with concomitant aberrantly shaped cristae. Together, this demonstrates that the unique macromolecular arrangement is critical for the maintenance of cristae morphology in Apicomplexa.
History
DepositionDec 4, 2019Deposition site: PDBE / Processing site: PDBE
Revision 1.0Dec 16, 2020Provider: repository / Type: Initial release
Revision 1.1Jan 20, 2021Group: Database references / Category: citation / citation_author
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year / _citation_author.identifier_ORCID / _citation_author.name

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Structure visualization

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  • Deposited structure unit
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Assembly

Deposited unit
q7: ATPTG11
i7: ATPTG7
t7: ATPTG14
g7: ATPTG5
o7: subunit k
k7: subunit a
j7: subunit i/j
s7: ATPTG13
u7: ATPTG15
h7: ATPTG6
e7: ATPTG3
x7: ATPTG17,ATPTG17,ATPTG17
b7: subunit b
r7: ATPTG12
p7: ATPTG10
v7: subunit f
l7: ATPTG8
c7: ATPTG1
d7: ATPTG2
m7: subunit 8
n7: ATPTG9
f7: ATPTG4
w7: ATPTG16
a7: subunit d
Q7: ATPTG11
I7: ATPTG7
T7: ATPTG14
G7: ATPTG5
O7: subunit k
K7: subunit a
J7: subunit i/j
S7: ATPTG13
U7: ATPTG15
H7: ATPTG6
E7: ATPTG3
X7: ATPTG17,ATPTG17,ATPTG17
B7: subunit b
R7: ATPTG12
P7: ATPTG10
V7: subunit f
L7: ATPTG8
C7: ATPTG1
D7: ATPTG2
M7: subunit 8
N7: ATPTG9
F7: ATPTG4
W7: ATPTG16
A7: subunit d
G1: Oligomycin sensitivity conferring protein (OSCP)
G2: Oligomycin sensitivity conferring protein (OSCP)
i1: Inhibitor of F1
A1: ATP synthase subunit alpha
E1: ATP synthase subunit alpha
C1: ATP synthase subunit alpha
B1: ATP synthase subunit beta
F1: ATP synthase subunit beta
D1: ATP synthase subunit beta
g1: ATP synthase subunit gamma
d1: ATP synthase subunit delta
e1: ATP synthase subunit epsilon
H1: subunit c
I1: subunit c
J1: subunit c
K1: subunit c
L1: subunit c
M1: subunit c
N1: subunit c
O1: subunit c
P1: subunit c
Q1: subunit c
i2: Inhibitor of F1
A2: ATP synthase subunit alpha
E2: ATP synthase subunit alpha
C2: ATP synthase subunit alpha
B2: ATP synthase subunit beta
F2: ATP synthase subunit beta
D2: ATP synthase subunit beta
g2: ATP synthase subunit gamma
d2: ATP synthase subunit delta
e2: ATP synthase subunit epsilon
H2: subunit c
I2: subunit c
J2: subunit c
K2: subunit c
L2: subunit c
M2: subunit c
N2: subunit c
O2: subunit c
P2: subunit c
Q2: subunit c
q8: ATPTG11
i8: ATPTG7
t8: ATPTG14
g8: ATPTG5
o8: subunit k
k8: subunit a
j8: subunit i/j
s8: ATPTG13
u8: ATPTG15
h8: ATPTG6
e8: ATPTG3
x8: ATPTG17,ATPTG17,ATPTG17
b8: subunit b
r8: ATPTG12
p8: ATPTG10
v8: subunit f
l8: ATPTG8
c8: ATPTG1
d8: ATPTG2
m8: subunit 8
n8: ATPTG9
f8: ATPTG4
w8: ATPTG16
a8: subunit d
Q8: ATPTG11
I8: ATPTG7
T8: ATPTG14
G8: ATPTG5
O8: subunit k
K8: subunit a
J8: subunit i/j
S8: ATPTG13
U8: ATPTG15
H8: ATPTG6
E8: ATPTG3
X8: ATPTG17,ATPTG17,ATPTG17
B8: subunit b
R8: ATPTG12
P8: ATPTG10
V8: subunit f
L8: ATPTG8
C8: ATPTG1
D8: ATPTG2
M8: subunit 8
N8: ATPTG9
F8: ATPTG4
W8: ATPTG16
A8: subunit d
G3: Oligomycin sensitivity conferring protein (OSCP)
G4: Oligomycin sensitivity conferring protein (OSCP)
i3: Inhibitor of F1
A3: ATP synthase subunit alpha
E3: ATP synthase subunit alpha
C3: ATP synthase subunit alpha
B3: ATP synthase subunit beta
F3: ATP synthase subunit beta
D3: ATP synthase subunit beta
g3: ATP synthase subunit gamma
d3: ATP synthase subunit delta
e3: ATP synthase subunit epsilon
H3: subunit c
I3: subunit c
J3: subunit c
K3: subunit c
L3: subunit c
M3: subunit c
N3: subunit c
O3: subunit c
P3: subunit c
Q3: subunit c
i4: Inhibitor of F1
A4: ATP synthase subunit alpha
E4: ATP synthase subunit alpha
C4: ATP synthase subunit alpha
B4: ATP synthase subunit beta
F4: ATP synthase subunit beta
D4: ATP synthase subunit beta
g4: ATP synthase subunit gamma
d4: ATP synthase subunit delta
e4: ATP synthase subunit epsilon
H4: subunit c
I4: subunit c
J4: subunit c
K4: subunit c
L4: subunit c
M4: subunit c
N4: subunit c
O4: subunit c
P4: subunit c
Q4: subunit c
q9: ATPTG11
i9: ATPTG7
t9: ATPTG14
g9: ATPTG5
o9: subunit k
k9: subunit a
j9: subunit i/j
s9: ATPTG13
u9: ATPTG15
h9: ATPTG6
e9: ATPTG3
x9: ATPTG17,ATPTG17,ATPTG17
b9: subunit b
r9: ATPTG12
p9: ATPTG10
v9: subunit f
l9: ATPTG8
c9: ATPTG1
d9: ATPTG2
m9: subunit 8
n9: ATPTG9
f9: ATPTG4
w9: ATPTG16
a9: subunit d
Q9: ATPTG11
I9: ATPTG7
T9: ATPTG14
G9: ATPTG5
O9: subunit k
K9: subunit a
J9: subunit i/j
S9: ATPTG13
U9: ATPTG15
H9: ATPTG6
E9: ATPTG3
X9: ATPTG17,ATPTG17,ATPTG17
B9: subunit b
R9: ATPTG12
P9: ATPTG10
V9: subunit f
L9: ATPTG8
C9: ATPTG1
D9: ATPTG2
M9: subunit 8
N9: ATPTG9
F9: ATPTG4
W9: ATPTG16
A9: subunit d
G5: Oligomycin sensitivity conferring protein (OSCP)
G6: Oligomycin sensitivity conferring protein (OSCP)
i5: Inhibitor of F1
A5: ATP synthase subunit alpha
E5: ATP synthase subunit alpha
C5: ATP synthase subunit alpha
B5: ATP synthase subunit beta
F5: ATP synthase subunit beta
D5: ATP synthase subunit beta
g5: ATP synthase subunit gamma
d5: ATP synthase subunit delta
e5: ATP synthase subunit epsilon
H5: subunit c
I5: subunit c
J5: subunit c
K5: subunit c
L5: subunit c
M5: subunit c
N5: subunit c
O5: subunit c
P5: subunit c
Q5: subunit c
i6: Inhibitor of F1
A6: ATP synthase subunit alpha
E6: ATP synthase subunit alpha
C6: ATP synthase subunit alpha
B6: ATP synthase subunit beta
F6: ATP synthase subunit beta
D6: ATP synthase subunit beta
g6: ATP synthase subunit gamma
d6: ATP synthase subunit delta
e6: ATP synthase subunit epsilon
H6: subunit c
I6: subunit c
J6: subunit c
K6: subunit c
L6: subunit c
M6: subunit c
N6: subunit c
O6: subunit c
P6: subunit c
Q6: subunit c


Theoretical massNumber of molelcules
Total (without water)7,546,032270
Polymers7,546,032270
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: microscopy
TypeNameSymmetry operationNumber
identity operation1_5551

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Components

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Protein , 27 types, 216 molecules q7Q7q8Q8q9Q9i7I7i8I8i9I9t7T7t8T8t9T9g7G7g8G8g9G9o7O7o8O8o9O9...

#1: Protein
ATPTG11


Mass: 15425.367 Da / Num. of mol.: 6 / Source method: isolated from a natural source
Source: (natural) Toxoplasma gondii (strain ATCC 50853 / GT1) (eukaryote)
Strain: ATCC 50853 / GT1 / References: UniProt: A0A125YPS4
#2: Protein
ATPTG7


Mass: 26866.773 Da / Num. of mol.: 6 / Source method: isolated from a natural source
Source: (natural) Toxoplasma gondii (strain ATCC 50853 / GT1) (eukaryote)
Strain: ATCC 50853 / GT1 / References: UniProt: S7VXW3
#3: Protein
ATPTG14


Mass: 14424.515 Da / Num. of mol.: 6 / Source method: isolated from a natural source
Source: (natural) Toxoplasma gondii (strain ATCC 50853 / GT1) (eukaryote)
Strain: ATCC 50853 / GT1 / References: UniProt: A0A125YLH9
#4: Protein
ATPTG5


Mass: 28162.615 Da / Num. of mol.: 6 / Source method: isolated from a natural source
Source: (natural) Toxoplasma gondii (strain ATCC 50853 / GT1) (eukaryote)
Strain: ATCC 50853 / GT1 / References: UniProt: S7WD71
#5: Protein
subunit k


Mass: 17963.504 Da / Num. of mol.: 6 / Source method: isolated from a natural source
Source: (natural) Toxoplasma gondii (strain ATCC 50853 / GT1) (eukaryote)
Strain: ATCC 50853 / GT1 / References: UniProt: A0A125YTD7
#6: Protein
subunit a


Mass: 24562.570 Da / Num. of mol.: 6 / Source method: isolated from a natural source
Source: (natural) Toxoplasma gondii (strain ATCC 50853 / GT1) (eukaryote)
Strain: ATCC 50853 / GT1 / References: UniProt: A0A125YSI9
#7: Protein
subunit i/j


Mass: 26600.543 Da / Num. of mol.: 6 / Source method: isolated from a natural source
Source: (natural) Toxoplasma gondii (strain ATCC 50853 / GT1) (eukaryote)
Strain: ATCC 50853 / GT1 / References: UniProt: S7UQ82
#8: Protein
ATPTG13


Mass: 14923.235 Da / Num. of mol.: 6 / Source method: isolated from a natural source
Source: (natural) Toxoplasma gondii (strain ATCC 50853 / GT1) (eukaryote)
Strain: ATCC 50853 / GT1 / References: UniProt: A0A125YLN4
#9: Protein
ATPTG15


Mass: 13871.887 Da / Num. of mol.: 6 / Source method: isolated from a natural source
Source: (natural) Toxoplasma gondii (strain ATCC 50853 / GT1) (eukaryote)
Strain: ATCC 50853 / GT1 / References: UniProt: A0A125YRP0
#10: Protein
ATPTG6


Mass: 27477.523 Da / Num. of mol.: 6 / Source method: isolated from a natural source
Source: (natural) Toxoplasma gondii (strain ATCC 50853 / GT1) (eukaryote)
Strain: ATCC 50853 / GT1 / References: UniProt: A0A125YL08
#11: Protein
ATPTG3


Mass: 35159.238 Da / Num. of mol.: 6 / Source method: isolated from a natural source
Source: (natural) Toxoplasma gondii (strain ATCC 50853 / GT1) (eukaryote)
Strain: ATCC 50853 / GT1 / References: UniProt: A0A125YLR0
#12: Protein
ATPTG17,ATPTG17,ATPTG17


Mass: 9486.748 Da / Num. of mol.: 6 / Source method: isolated from a natural source
Source: (natural) Toxoplasma gondii (strain ATCC 50853 / GT1) (eukaryote), (natural) Toxoplasma gondii GT1 (eukaryote)
Strain: ATCC 50853 / GT1 / References: UniProt: S7W180
#13: Protein
subunit b


Mass: 64811.602 Da / Num. of mol.: 6 / Source method: isolated from a natural source
Source: (natural) Toxoplasma gondii (strain ATCC 50853 / GT1) (eukaryote)
Strain: ATCC 50853 / GT1 / References: UniProt: S7V2T0
#14: Protein
ATPTG12


Mass: 15400.639 Da / Num. of mol.: 6 / Source method: isolated from a natural source
Source: (natural) Toxoplasma gondii (strain ATCC 50853 / GT1) (eukaryote)
Strain: ATCC 50853 / GT1 / References: UniProt: A0A125YKF7
#15: Protein
ATPTG10


Mass: 15165.213 Da / Num. of mol.: 6 / Source method: isolated from a natural source
Source: (natural) Toxoplasma gondii (strain ATCC 50853 / GT1) (eukaryote)
Strain: ATCC 50853 / GT1 / References: UniProt: A0A125YMA7
#16: Protein
subunit f


Mass: 13029.997 Da / Num. of mol.: 6 / Source method: isolated from a natural source
Source: (natural) Toxoplasma gondii (strain ATCC 50853 / GT1) (eukaryote)
Strain: ATCC 50853 / GT1 / References: UniProt: S7UQT7
#17: Protein
ATPTG8


Mass: 23365.865 Da / Num. of mol.: 6 / Source method: isolated from a natural source
Source: (natural) Toxoplasma gondii (strain ATCC 50853 / GT1) (eukaryote)
Strain: ATCC 50853 / GT1 / References: UniProt: S7W7F1
#18: Protein
ATPTG1


Mass: 46025.355 Da / Num. of mol.: 6 / Source method: isolated from a natural source
Source: (natural) Toxoplasma gondii (strain ATCC 50853 / GT1) (eukaryote)
Strain: ATCC 50853 / GT1 / References: UniProt: S7W9J5
#19: Protein
ATPTG2


Mass: 35238.520 Da / Num. of mol.: 6 / Source method: isolated from a natural source
Source: (natural) Toxoplasma gondii (strain ATCC 50853 / GT1) (eukaryote)
Strain: ATCC 50853 / GT1 / References: UniProt: A0A125YV76
#20: Protein
subunit 8


Mass: 22344.648 Da / Num. of mol.: 6 / Source method: isolated from a natural source
Source: (natural) Toxoplasma gondii (strain ATCC 50853 / GT1) (eukaryote)
Strain: ATCC 50853 / GT1 / References: UniProt: A0A125YPQ4
#21: Protein
ATPTG9


Mass: 18426.826 Da / Num. of mol.: 6 / Source method: isolated from a natural source
Source: (natural) Toxoplasma gondii (strain ATCC 50853 / GT1) (eukaryote)
Strain: ATCC 50853 / GT1 / References: UniProt: A0A125YUZ2
#22: Protein
ATPTG4


Mass: 28557.363 Da / Num. of mol.: 6 / Source method: isolated from a natural source
Source: (natural) Toxoplasma gondii (strain ATCC 50853 / GT1) (eukaryote)
Strain: ATCC 50853 / GT1 / References: UniProt: S7UVZ7
#23: Protein
ATPTG16


Mass: 11587.373 Da / Num. of mol.: 6 / Source method: isolated from a natural source
Source: (natural) Toxoplasma gondii (strain ATCC 50853 / GT1) (eukaryote)
Strain: ATCC 50853 / GT1 / References: UniProt: S7VTI0
#24: Protein
subunit d


Mass: 61362.250 Da / Num. of mol.: 6 / Source method: isolated from a natural source
Source: (natural) Toxoplasma gondii (strain ATCC 50853 / GT1) (eukaryote)
Strain: ATCC 50853 / GT1 / References: UniProt: S7V493
#25: Protein
Oligomycin sensitivity conferring protein (OSCP)


Mass: 27669.994 Da / Num. of mol.: 6 / Source method: isolated from a natural source
Source: (natural) Toxoplasma gondii (strain ATCC 50853 / GT1) (eukaryote)
Strain: ATCC 50853 / GT1 / References: UniProt: A0A125YKF8
#26: Protein
Inhibitor of F1


Mass: 16167.462 Da / Num. of mol.: 6 / Source method: isolated from a natural source
Source: (natural) Toxoplasma gondii (strain ATCC 50853 / GT1) (eukaryote)
Strain: ATCC 50853 / GT1 / References: UniProt: A0A125YJP2
#32: Protein ...
subunit c


Mass: 17753.504 Da / Num. of mol.: 60 / Source method: isolated from a natural source
Source: (natural) Toxoplasma gondii (strain ATCC 50853 / GT1) (eukaryote)
Strain: ATCC 50853 / GT1 / References: UniProt: A0A125YJV2

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ATP synthase subunit ... , 5 types, 54 molecules A1E1C1A2E2C2A3E3C3A4E4C4A5E5C5A6E6C6B1F1D1B2F2D2B3F3D3B4F4D4...

#27: Protein
ATP synthase subunit alpha /


Mass: 61189.168 Da / Num. of mol.: 18 / Source method: isolated from a natural source
Source: (natural) Toxoplasma gondii (strain ATCC 50853 / GT1) (eukaryote), (natural) Toxoplasma gondii GT1 (eukaryote)
Strain: ATCC 50853 / GT1 / References: UniProt: S7UU80
#28: Protein
ATP synthase subunit beta /


Mass: 59983.316 Da / Num. of mol.: 18 / Source method: isolated from a natural source
Source: (natural) Toxoplasma gondii (strain ATCC 50853 / GT1) (eukaryote)
Strain: ATCC 50853 / GT1
References: UniProt: A0A125YYY4, H+-transporting two-sector ATPase
#29: Protein
ATP synthase subunit gamma /


Mass: 34573.031 Da / Num. of mol.: 6 / Source method: isolated from a natural source
Source: (natural) Toxoplasma gondii (strain ATCC 50853 / GT1) (eukaryote)
Strain: ATCC 50853 / GT1 / References: UniProt: A0A125YUH0
#30: Protein
ATP synthase subunit delta /


Mass: 19476.082 Da / Num. of mol.: 6 / Source method: isolated from a natural source
Source: (natural) Toxoplasma gondii (strain ATCC 50853 / GT1) (eukaryote)
Strain: ATCC 50853 / GT1 / References: UniProt: A0A125YRE2
#31: Protein
ATP synthase subunit epsilon /


Mass: 8492.709 Da / Num. of mol.: 6 / Source method: isolated from a natural source
Source: (natural) Toxoplasma gondii (strain ATCC 50853 / GT1) (eukaryote)
Strain: ATCC 50853 / GT1 / References: UniProt: S7VV10

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

ComponentName: Toxoplasma gondii ATP synthase hexamer / Type: COMPLEX / Entity ID: all / Source: NATURAL
Molecular weightValue: 5.6 MDa / Experimental value: NO
Source (natural)Organism: Toxoplasma gondii GT1 (eukaryote)
Buffer solutionpH: 7.5
SpecimenConc.: 19 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
Specimen supportGrid material: COPPER / Grid type: Quantifoil R1.2/1.3
VitrificationInstrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: FEI TITAN KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELDBright-field microscopy / Nominal magnification: 130000 X / Cs: 2.7 mm
Specimen holderCryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER
Image recordingElectron dose: 32 e/Å2 / Detector mode: COUNTING / Film or detector model: GATAN K2 QUANTUM (4k x 4k) / Num. of real images: 7604
EM imaging opticsEnergyfilter name: GIF Quantum LS / Energyfilter slit width: 20 eV
Image scansMovie frames/image: 20

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Processing

EM software
IDNameVersionCategory
1Gautomatchparticle selection
2EPUimage acquisition
4GctfCTF correction
9RELION3initial Euler assignment
10RELION3final Euler assignment
12RELION33D reconstruction
13PHENIX1.17rc2-3612model refinement
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Particle selectionNum. of particles selected: 26542
SymmetryPoint symmetry: C3 (3 fold cyclic)
3D reconstructionResolution: 4.8 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 4532 / Algorithm: FOURIER SPACE / Symmetry type: POINT
Atomic model buildingSpace: REAL

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