PDB-7nkq: Mycobacterium smegmatis ATP synthase b-delta state 3

基本情報

• 登録情報: データベース: PDB / ID: 7nkq
• タイトル: Mycobacterium smegmatis ATP synthase b-delta state 3

要素

• ATP synthase subunit alpha
• ATP synthase subunit b
• ATP synthase subunit b-delta
• ATP synthase subunit beta

• キーワード: HYDROLASE / complex / synthase

機能・相同性

分子機能:

proton-transporting ATP synthase complex, coupling factor F(o) / photosynthetic electron transport in photosystem I / proton-transporting ATP synthase complex, catalytic core F(1) / photosynthetic electron transport in photosystem II / H+-transporting two-sector ATPase / proton-transporting ATPase activity, rotational mechanism / proton-transporting ATP synthase activity, rotational mechanism / ADP binding / ATP hydrolysis activity / ATP binding / plasma membrane

ドメイン・相同性:

ATP synthase, F0 complex, subunit b, bacterial / F-type ATP synthase subunit B-like, membrane domain superfamily / ATP synthase, F0 complex, subunit b/b', bacterial/chloroplast / ATP synthase B/B' CF(0) / ATPase, OSCP/delta subunit / ATP synthase delta (OSCP) subunit / ATP synthase, F1 complex, beta subunit / ATP synthase, alpha subunit, C-terminal domain superfamily / 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 / 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 / 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. / ATPase, F1/V1/A1 complex, alpha/beta subunit, nucleotide-binding domain / ATP synthase alpha/beta family, nucleotide-binding domain / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / P-loop containing nucleoside triphosphate hydrolase

構成要素:

ATP synthase subunit beta / ATP synthase subunit alpha / ATP synthase subunit b-delta / ATP synthase subunit b

• 生物種: Mycolicibacterium smegmatis MC2 155 (バクテリア)
• 手法: 電子顕微鏡法 / 単粒子再構成法 / クライオ電子顕微鏡法 / 解像度: 2.98 Å
• データ登録者: Montgomery, M.G. / Petri, J. / Spikes, T.E. / Walker, J.E.

資金援助

英国, 2件

組織	認可番号	国
Medical Research Council (MRC, United Kingdom)	MR/M009858/1	英国
Medical Research Council (MRC, United Kingdom)	MC_UU_00015/8	英国

• 引用: ジャーナル: Proc Natl Acad Sci U S A / 年: 2021; タイトル: Structure of the ATP synthase from provides targets for treating tuberculosis.; 著者: Martin G Montgomery / Jessica Petri / Tobias E Spikes / John E Walker / ; 要旨: The structure has been determined by electron cryomicroscopy of the adenosine triphosphate (ATP) synthase from This analysis confirms features in a prior description of the structure of the enzyme, but it also describes other highly significant attributes not recognized before that are crucial for understanding the mechanism and regulation of the mycobacterial enzyme. First, we resolved not only the three main states in the catalytic cycle described before but also eight substates that portray structural and mechanistic changes occurring during a 360° catalytic cycle. Second, a mechanism of auto-inhibition of ATP hydrolysis involves not only the engagement of the C-terminal region of an α-subunit in a loop in the γ-subunit, as proposed before, but also a "fail-safe" mechanism involving the b'-subunit in the peripheral stalk that enhances engagement. A third unreported characteristic is that the fused bδ-subunit contains a duplicated domain in its N-terminal region where the two copies of the domain participate in similar modes of attachment of the two of three N-terminal regions of the α-subunits. The auto-inhibitory plus the associated "fail-safe" mechanisms and the modes of attachment of the α-subunits provide targets for development of innovative antitubercular drugs. The structure also provides support for an observation made in the bovine ATP synthase that the transmembrane proton-motive force that provides the energy to drive the rotary mechanism is delivered directly and tangentially to the rotor via a Grotthuss water chain in a polar L-shaped tunnel.

履歴

登録	2021年2月18日	登録サイト: PDBE / 処理サイト: PDBE
改定 1.0	2021年10月27日	Provider: repository / タイプ: Initial release
改定 1.1	2021年11月24日	Group: Database references / カテゴリ: citation / citation_author Item: _citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year
改定 1.2	2024年7月10日	Group: Data collection / カテゴリ: chem_comp_atom / chem_comp_bond / em_admin / Item: _em_admin.last_update