- PDB-6tmk: Cryo-EM structure of Toxoplasma gondii mitochondrial ATP synthase... -
+
データを開く
IDまたはキーワード:
読み込み中...
-
基本情報
登録情報
データベース: PDB / ID: 6tmk
タイトル
Cryo-EM structure of Toxoplasma gondii mitochondrial ATP synthase dimer, composite model
要素
(ATP synthase subunit ...) x 5
ATPTG1
ATPTG10
ATPTG11
ATPTG12
ATPTG13
ATPTG14
ATPTG15
ATPTG16
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
キーワード
MEMBRANE PROTEIN / mitochondrial / ATP synthase / dimer / lipids
機能・相同性
機能・相同性情報
thylakoid / mitochondrial electron transport, ubiquinol to cytochrome c / proton transmembrane transporter activity / proton motive force-driven ATP synthesis / proton-transporting two-sector ATPase complex, proton-transporting domain / proton motive force-driven mitochondrial ATP synthesis / H+-transporting two-sector ATPase / proton-transporting ATP synthase complex / proton-transporting ATP synthase activity, rotational mechanism / ADP binding ...thylakoid / mitochondrial electron transport, ubiquinol to cytochrome c / proton transmembrane transporter activity / proton motive force-driven ATP synthesis / proton-transporting two-sector ATPase complex, proton-transporting domain / proton motive force-driven mitochondrial ATP synthesis / H+-transporting two-sector ATPase / proton-transporting ATP synthase complex / proton-transporting ATP synthase activity, rotational mechanism / ADP binding / electron transfer activity / hydrolase activity / mitochondrial inner membrane / heme binding / lipid binding / ATP hydrolysis activity / ATP binding / metal ion binding / membrane 類似検索 - 分子機能
: / : / ATPTG10-like / Apicomplexa microprotein / ATP synthase, F0 complex, subunit D superfamily, mitochondrial / Cytochrome c1, transmembrane anchor, C-terminal / Cytochrome c1 / Cytochrome C1 family / ATP synthase, F1 complex, epsilon subunit, mitochondrial / ATP synthase, F1 complex, epsilon subunit superfamily, mitochondrial ...: / : / ATPTG10-like / Apicomplexa microprotein / ATP synthase, F0 complex, subunit D superfamily, mitochondrial / Cytochrome c1, transmembrane anchor, C-terminal / 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 / F1F0 ATP synthase OSCP/delta subunit, N-terminal domain superfamily / Thioredoxin / 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, F1 complex, alpha subunit nucleotide-binding domain / ATP synthase, alpha subunit, C-terminal / ATP synthase, F1 complex, alpha subunit / 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
ADENOSINE-5'-DIPHOSPHATE / ADENOSINE-5'-TRIPHOSPHATE / CARDIOLIPIN / 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE / 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine / Uncharacterized protein / Putative ATP synthase F0 subunit 9 / Uncharacterized protein / ATP synthase F1, delta subunit protein / NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7 ...ADENOSINE-5'-DIPHOSPHATE / ADENOSINE-5'-TRIPHOSPHATE / CARDIOLIPIN / 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE / 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine / 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 / Microprotein domain-containing 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.
履歴
登録
2019年12月4日
登録サイト: PDBE / 処理サイト: PDBE
改定 1.0
2020年12月16日
Provider: repository / タイプ: Initial release
改定 1.0
2020年12月16日
Data content type: EM metadata / Data content type: EM metadata / Provider: repository / タイプ: Initial release
改定 1.0
2020年12月16日
Data content type: FSC / Data content type: FSC / Provider: repository / タイプ: Initial release
改定 1.0
2020年12月16日
Data content type: Half map / Part number: 1 / Data content type: Half map / Provider: repository / タイプ: Initial release
改定 1.0
2020年12月16日
Data content type: Half map / Part number: 2 / Data content type: Half map / Provider: repository / タイプ: Initial release
改定 1.0
2020年12月16日
Data content type: Image / Data content type: Image / Provider: repository / タイプ: Initial release
改定 1.0
2020年12月16日
Data content type: Mask / Data content type: Mask / Provider: repository / タイプ: Initial release
改定 1.0
2020年12月16日
Data content type: Primary map / Data content type: Primary map / Provider: repository / タイプ: Initial release
改定 1.0
2020年12月16日
Data content type: EM metadata / Data content type: EM metadata / Provider: repository / タイプ: Initial release
改定 1.0
2020年12月16日
Data content type: FSC / Data content type: FSC / Provider: repository / タイプ: Initial release
改定 1.0
2020年12月16日
Data content type: Half map / Part number: 1 / Data content type: Half map / Provider: repository / タイプ: Initial release
改定 1.0
2020年12月16日
Data content type: Half map / Part number: 2 / Data content type: Half map / Provider: repository / タイプ: Initial release
改定 1.0
2020年12月16日
Data content type: Image / Data content type: Image / Provider: repository / タイプ: Initial release
改定 1.0
2020年12月16日
Data content type: Mask / Data content type: Mask / Provider: repository / タイプ: Initial release
改定 1.0
2020年12月16日
Data content type: Primary map / Data content type: Primary map / Provider: repository / タイプ: Initial release
Data content type: EM metadata / Data content type: EM metadata / EM metadata / EM metadata Group: Database references / Experimental summary / Structure summary Data content type: EM metadata / EM metadata / EM metadata / カテゴリ: database_2 / em_admin / entity Data content type: EM metadata / EM metadata ...EM metadata / EM metadata / EM metadata / EM metadata / EM metadata / EM metadata Item: _chem_comp.name / _database_2.pdbx_DOI ..._chem_comp.name / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _em_admin.last_update / _entity.formula_weight / _entity.pdbx_description