- EMDB-10525: Cryo-EM structure of Toxoplasma gondii mitochondrial ATP synthase... -
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基本情報
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データベース: EMDB / ID: EMD-10525
タイトル
Cryo-EM structure of Toxoplasma gondii mitochondrial ATP synthase hexamer, membrane region
マップデータ
Toxoplasma gondii ATP synthase hexamer, membrane region
試料
複合体: Toxoplasma gondii ATP synthase hexamer
タンパク質・ペプチド: x 32種
機能・相同性
機能・相同性情報
thylakoid / : / : / : / proton-transporting ATP synthase complex, coupling factor F(o) / proton motive force-driven ATP synthesis / proton motive force-driven mitochondrial ATP synthesis / proton transmembrane transporter activity / proton-transporting ATP synthase complex, catalytic core F(1) / H+-transporting two-sector ATPase ...thylakoid / : / : / : / proton-transporting ATP synthase complex, coupling factor F(o) / proton motive force-driven ATP synthesis / proton motive force-driven mitochondrial ATP synthesis / proton transmembrane transporter activity / 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 / chloroplast / ADP binding / mitochondrial inner membrane / electron transfer activity / hydrolase activity / lipid binding / heme binding / ATP hydrolysis activity / ATP binding / membrane / metal ion binding 類似検索 - 分子機能
: / ATPTG10-like / Cytochrome c1, transmembrane anchor, C-terminal / ATP synthase, F0 complex, subunit D superfamily, mitochondrial / Cytochrome c1 / Cytochrome C1 family / 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 / ATP synthase, F0 complex, subunit D superfamily, mitochondrial / Cytochrome c1 / Cytochrome C1 family / 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 / C-terminal domain of V and A type ATP synthase / ATP synthase subunit alpha, N-terminal domain-like superfamily / ATPase, F1/V1/A1 complex, alpha/beta subunit, N-terminal domain superfamily / 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 family profile. / Cytochrome c-like domain / 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 類似検索 - ドメイン・相同性
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 類似検索 - 構成要素
ジャーナル: Nat Commun / 年: 2021 タイトル: ATP synthase hexamer assemblies shape cristae of Toxoplasma mitochondria. 著者: Alexander Mühleip / Rasmus Kock Flygaard / Jana Ovciarikova / Alice Lacombe / Paula Fernandes / Lilach Sheiner / Alexey Amunts / 要旨: 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.
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基本情報
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機能・相同性情報
Toxoplasma gondii GT1 (トキソプラズマ) / 
データ登録者
スウェーデン, 4件 
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emd_10525.png
http://ftp.pdbj.org/pub/emdb/structures/EMD-10525
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