EMDB/PDB/SASBDBから引用されている文献のデータベース

キーワード
構造解析手法	All X線回折 NMR 電子顕微鏡小角散乱中性子線回折線維回折粉末回折赤外分光 EPR FRET 理論モデルハイブリッド
著者・登録者
ジャーナル
IF	>30 >20 >10 >5 all

タイトル	A structural framework for unidirectional transport by a bacterial ABC exporter.
ジャーナル・号・ページ	Proc Natl Acad Sci U S A, Vol. 117, Issue 32, Page 19228-19236, Year 2020
掲載日	2020年8月11日
著者	Chengcheng Fan / Jens T Kaiser / Douglas C Rees /
PubMed 要旨	The ATP-binding cassette (ABC) transporter of mitochondria (Atm1) mediates iron homeostasis in eukaryotes, while the prokaryotic homolog from (Atm1) can export glutathione derivatives and confer ...The ATP-binding cassette (ABC) transporter of mitochondria (Atm1) mediates iron homeostasis in eukaryotes, while the prokaryotic homolog from (Atm1) can export glutathione derivatives and confer protection against heavy-metal toxicity. To establish the structural framework underlying the Atm1 transport mechanism, we determined eight structures by X-ray crystallography and single-particle cryo-electron microscopy in distinct conformational states, stabilized by individual disulfide crosslinks and nucleotides. As Atm1 progresses through the transport cycle, conformational changes in transmembrane helix 6 (TM6) alter the glutathione-binding site and the associated substrate-binding cavity. Significantly, kinking of TM6 in the post-ATP hydrolysis state stabilized by MgADPVO eliminates this cavity, precluding uptake of glutathione derivatives. The presence of this cavity during the transition from the inward-facing to outward-facing conformational states, and its absence in the reverse direction, thereby provide an elegant and conceptually simple mechanism for enforcing the export directionality of transport by Atm1. One of the disulfide crosslinked Atm1 variants characterized in this work retains significant glutathione transport activity, suggesting that ATP hydrolysis and substrate transport by Atm1 may involve a limited set of conformational states with minimal separation of the nucleotide-binding domains in the inward-facing conformation.
リンク	Proc Natl Acad Sci U S A / PubMed:32703810 / PubMed Central
手法	EM (単粒子) / X線回折
解像度	3.03 - 3.88 Å
構造データ	21356 6vqt EMDB-21356, PDB-6vqt: Structure of a bacterial Atm1-family ABC exporter with MgADPVO4 bound 手法: EM (単粒子) / 解像度: 3.03 Å 21357 6vqu EMDB-21357, PDB-6vqu: Structure of a bacterial Atm1-family ABC exporter 手法: EM (単粒子) / 解像度: 3.88 Å PDB-6pam: Structure of a bacterial Atm1-family ABC transporter with MgADP bound 手法: X-RAY DIFFRACTION / 解像度: 3.7 Å PDB-6pan: Structure of a bacterial Atm1-family ABC exporter with ATP bound 手法: X-RAY DIFFRACTION / 解像度: 3.4 Å PDB-6pao: Structure of a bacterial Atm1-family ABC exporter with ATP bound 手法: X-RAY DIFFRACTION / 解像度: 3.65 Å PDB-6paq: Structure of a bacterial Atm1-family ABC exporter with ATP bound 手法: X-RAY DIFFRACTION / 解像度: 3.301 Å PDB-6par: Structure of a bacterial Atm1-family ABC exporter with MgAMPPNP bound 手法: X-RAY DIFFRACTION / 解像度: 3.35 Å
化合物	ChemComp-ADP: ADENOSINE-5'-DIPHOSPHATE / ADP / ADP, エネルギー貯蔵分子YM / アデノシン二リン酸 ChemComp-MG: Unknown entry / マグネシウムジカチオン ChemComp-ATP: ADENOSINE-5'-TRIPHOSPHATE / ATP / ATP, エネルギー貯蔵分子YM / アデノシン三リン酸 ChemComp-ANP: PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / AMP-PNP / AMP-PNP, エネルギー貯蔵分子類似体YM ChemComp-VO4*: VANADATE ION / バナジン酸塩
由来	Novosphingobium aromaticivorans DSM 12444 (バクテリア) novosphingobium aromaticivorans (strain atcc 700278 / dsm 12444 / cip 105152 / nbrc 16084 / f199) (バクテリア)
キーワード	TRANSPORT PROTEIN (運搬体タンパク質) / ABC transporter / ABC exporter / ATPase (ATPアーゼ) / membrane protein (膜タンパク質)