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	Structural insights into substrate recognition and translocation of human peroxisomal ABC transporter ALDP.
ジャーナル・号・ページ	Signal Transduct Target Ther, Vol. 8, Issue 1, Page 74, Year 2023
掲載日	2023年2月22日
著者	Chao Xiong / Li-Na Jia / Wei-Xi Xiong / Xin-Tong Wu / Liu-Lin Xiong / Ting-Hua Wang / Dong Zhou / Zhen Hong / Zheng Liu / Lin Tang /
PubMed 要旨	Dysfunctions of ATP-binding cassette, subfamily D, member 1 (ABCD1) cause X-linked adrenoleukodystrophy, a rare neurodegenerative disease that affects all human tissues. Residing in the peroxisome ...Dysfunctions of ATP-binding cassette, subfamily D, member 1 (ABCD1) cause X-linked adrenoleukodystrophy, a rare neurodegenerative disease that affects all human tissues. Residing in the peroxisome membrane, ABCD1 plays a role in the translocation of very long-chain fatty acids for their β-oxidation. Here, the six cryo-electron microscopy structures of ABCD1 in four distinct conformational states were presented. In the transporter dimer, two transmembrane domains form the substrate translocation pathway, and two nucleotide-binding domains form the ATP-binding site that binds and hydrolyzes ATP. The ABCD1 structures provide a starting point for elucidating the substrate recognition and translocation mechanism of ABCD1. Each of the four inward-facing structures of ABCD1 has a vestibule that opens to the cytosol with variable sizes. Hexacosanoic acid (C26:0)-CoA substrate binds to the transmembrane domains (TMDs) and stimulates the ATPase activity of the nucleotide-binding domains (NBDs). W339 from the transmembrane helix 5 (TM5) is essential for binding substrate and stimulating ATP hydrolysis by substrate. ABCD1 has a unique C-terminal coiled-coil domain that negatively modulates the ATPase activity of the NBDs. Furthermore, the structure of ABCD1 in the outward-facing state indicates that ATP molecules pull the two NBDs together and open the TMDs to the peroxisomal lumen for substrate release. The five structures provide a view of the substrate transport cycle and mechanistic implication for disease-causing mutations.
リンク	Signal Transduct Target Ther / PubMed:36810450 / PubMed Central
手法	EM (単粒子)
解像度	2.96 - 3.78 Å
構造データ	32919 7x07 EMDB-32919, PDB-7x07: Cryo-EM structure of human ABCD1 in the presence of C26:0 手法: EM (単粒子) / 解像度: 3.78 Å 32924 7x0t EMDB-32924, PDB-7x0t: Cryo-EM structure of human ABCD1 E630Q in the presence of C26:0-CoA and ATP 手法: EM (単粒子) / 解像度: 3.3 Å 32930 7x0z EMDB-32930, PDB-7x0z: Cryo-EM structure of human ABCD1 E630Q in the presence of ATP and Magnesium in outward-facing state 手法: EM (単粒子) / 解像度: 2.96 Å 32951 7x1w EMDB-32951, PDB-7x1w: Cryo-EM structure of human ABCD1 E630Q in the presence of ATP in inward-facing state 手法: EM (単粒子) / 解像度: 3.3 Å 33155 7xec EMDB-33155, PDB-7xec: Cryo-EM structure of human ABCD1 E630Q in the presence of ATP in inward-facing state 2 手法: EM (単粒子) / 解像度: 3.34 Å 34064 7yrq EMDB-34064, PDB-7yrq: Cryo-EM structure of human Peroxisomal ABC Transporter ABCD1 手法: EM (単粒子) / 解像度: 3.35 Å
化合物	ChemComp-7PO: hexacosanoic acid / ヘキサコサン酸 ChemComp-CO8: OCTANOYL-COENZYME A / オクタノイル-CoA / Octanoyl-CoA 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-MG: Unknown entry / マグネシウムジカチオン ChemComp-K9G*: [(2~{R})-1-hexadecanoyloxy-3-[oxidanyl-[2-(trimethyl-$l^{4}-azanyl)ethoxy]phosphoryl]oxy-propan-2-yl] octadec-9-enoate
由来	homo sapiens (ヒト)
キーワード	STRUCTURAL PROTEIN (タンパク質) / complex / Membrane protein (膜タンパク質) / ligand (リガンド)