- EMDB-24184: Structure of AtAtm3 in the closed conformation -
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基本情報
登録情報
データベース: EMDB / ID: EMD-24184
タイトル
Structure of AtAtm3 in the closed conformation
マップデータ
AtAtm3 in the closed conformation
試料
複合体: AtAtm3 in MSP nanodiscs
タンパク質・ペプチド: ABC transporter B family member 25, mitochondrial
リガンド: ADENOSINE-5'-DIPHOSPHATE
リガンド: VANADATE ION
リガンド: MAGNESIUM ION
キーワード
ABC transporter / ATPase / MEMBRANE PROTEIN
機能・相同性
機能・相同性情報
regulation of chlorophyll biosynthetic process / chloroplast organization / pollen development / root development / regulation of catalytic activity / Mo-molybdopterin cofactor biosynthetic process / chloroplast envelope / plastid / ABC-type transporter activity / chromosome organization ...regulation of chlorophyll biosynthetic process / chloroplast organization / pollen development / root development / regulation of catalytic activity / Mo-molybdopterin cofactor biosynthetic process / chloroplast envelope / plastid / ABC-type transporter activity / chromosome organization / response to cadmium ion / chloroplast / response to lead ion / iron ion transport / intracellular iron ion homeostasis / mitochondrial inner membrane / ATP hydrolysis activity / mitochondrion / ATP binding 類似検索 - 分子機能
Type 1 protein exporter / ABC transporter transmembrane region / ABC transporter type 1, transmembrane domain / ABC transporter integral membrane type-1 fused domain profile. / ABC transporter type 1, transmembrane domain superfamily / ABC transporter-like, conserved site / ABC transporters family signature. / ABC transporter / ABC transporter-like, ATP-binding domain / ATP-binding cassette, ABC transporter-type domain profile. ...Type 1 protein exporter / ABC transporter transmembrane region / ABC transporter type 1, transmembrane domain / ABC transporter integral membrane type-1 fused domain profile. / ABC transporter type 1, transmembrane domain superfamily / ABC transporter-like, conserved site / ABC transporters family signature. / ABC transporter / ABC transporter-like, ATP-binding domain / ATP-binding cassette, ABC transporter-type domain profile. / 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
ABC transporter B family member 25, mitochondrial 類似検索 - 構成要素
ジャーナル: Elife / 年: 2022 タイトル: Glutathione binding to the plant Atm3 transporter and implications for the conformational coupling of ABC transporters. 著者: Chengcheng Fan / Douglas C Rees / 要旨: The ATP binding cassette (ABC) transporter of mitochondria (Atm) from (Atm3) has been implicated in the maturation of cytosolic iron-sulfur proteins and heavy metal detoxification, plausibly by ...The ATP binding cassette (ABC) transporter of mitochondria (Atm) from (Atm3) has been implicated in the maturation of cytosolic iron-sulfur proteins and heavy metal detoxification, plausibly by exporting glutathione derivatives. Using single-particle cryo-electron microscopy, we have determined four structures of Atm3 in three different conformational states: two inward-facing conformations (with and without bound oxidized glutathione [GSSG]), together with closed and outward-facing states stabilized by MgADP-VO. These structures not only provide a structural framework for defining the alternating access transport cycle, but also reveal the paucity of cysteine residues in the glutathione binding site that could potentially form inhibitory mixed disulfides with GSSG. Despite extensive efforts, we were unable to prepare the ternary complex of Atm3 containing both GSSG and MgATP. A survey of structurally characterized type IV ABC transporters that includes Atm3 establishes that while nucleotides are found associated with all conformational states, they are effectively required to stabilize occluded, closed, and outward-facing conformations. In contrast, transport substrates have only been observed associated with inward-facing conformations. The absence of structures with dimerized nucleotide binding domains containing both nucleotide and transport substrate suggests that this form of the ternary complex exists only transiently during the transport cycle.