Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Structural insights into substrate recognition and translocation of human peroxisomal ABC transporter ALDP.
Journal, issue, pages	Signal Transduct Target Ther, Vol. 8, Issue 1, Page 74, Year 2023
Publish date	Feb 22, 2023
Authors	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 Abstract	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.
External links	Signal Transduct Target Ther / PubMed:36810450 / PubMed Central
Methods	EM (single particle)
Resolution	2.96 - 3.78 Å
Structure data	32919 7x07 EMDB-32919, PDB-7x07: Cryo-EM structure of human ABCD1 in the presence of C26:0 Method: EM (single particle) / Resolution: 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 Method: EM (single particle) / Resolution: 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 Method: EM (single particle) / Resolution: 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 Method: EM (single particle) / Resolution: 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 Method: EM (single particle) / Resolution: 3.34 Å 34064 7yrq EMDB-34064, PDB-7yrq: Cryo-EM structure of human Peroxisomal ABC Transporter ABCD1 Method: EM (single particle) / Resolution: 3.35 Å
Chemicals	ChemComp-7PO: hexacosanoic acid ChemComp-CO8: OCTANOYL-COENZYME A / Octanoyl-CoA ChemComp-ATP: ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying moleculeYM / Adenosine triphosphate ChemComp-MG: Unknown entry ChemComp-K9G*: [(2~{R})-1-hexadecanoyloxy-3-[oxidanyl-[2-(trimethyl-$l^{4}-azanyl)ethoxy]phosphoryl]oxy-propan-2-yl] octadec-9-enoate
Source	homo sapiens (human)
Keywords	STRUCTURAL PROTEIN / complex / Membrane protein / ligand