Cryo-EM structure of human lysosomal cobalamin exporter ABCD4
Dear Editor, Cobalamin, also known as vitamin B12, can only be biosynthesized by certain
bacteria and archaea. As an essential nutrient for humans, it should be obtained from daily …
bacteria and archaea. As an essential nutrient for humans, it should be obtained from daily …
[HTML][HTML] The lysosomal protein ABCD4 can transport vitamin B12 across liposomal membranes in vitro
K Kitai, K Kawaguchi, T Tomohiro, M Morita… - Journal of Biological …, 2021 - ASBMB
Vitamin B 12 (cobalamin) is an essential micronutrient for human health, and mutation and
dysregulation of cobalamin metabolism are associated with serious diseases, such as …
dysregulation of cobalamin metabolism are associated with serious diseases, such as …
[HTML][HTML] Clinical or ATPase domain mutations in ABCD4 disrupt the interaction between the vitamin B12-trafficking proteins ABCD4 and LMBD1
V Fettelschoss, P Burda, C Sagné, D Coelho… - Journal of Biological …, 2017 - ASBMB
Vitamin B 12 (cobalamin (Cbl)), in the cofactor forms methyl-Cbl and adenosyl-Cbl, is
required for the function of the essential enzymes methionine synthase and methylmalonyl …
required for the function of the essential enzymes methionine synthase and methylmalonyl …
Cryo-EM structure of AMP-PNP-bound human mitochondrial ATP-binding cassette transporter ABCB7
Q Yan, Y Shen, X Yang - Journal of Structural Biology, 2022 - Elsevier
ATP-binding cassette subfamily B member 7 (ABCB7) is localized in the inner membrane of
mitochondria, playing a critical role in iron metabolism. Here, we determined the structure of …
mitochondria, playing a critical role in iron metabolism. Here, we determined the structure of …
Cryo-EM structure of human bile salts exporter ABCB11
Dear Editor, Bile is a complex aqueous secretion produced by the liver that facilitates the
digestion of lipids in the small intestine. A group of ATP binding cassette (ABC) transporters …
digestion of lipids in the small intestine. A group of ATP binding cassette (ABC) transporters …
Substrate-induced transmembrane signaling in the cobalamin transporter BtuB
DP Chimento, AK Mohanty, RJ Kadner… - Nature Structural & …, 2003 - nature.com
The outer membranes of Gram-negative bacteria possess transport proteins essential for
uptake of scarce nutrients. In TonB-dependent transporters, a conserved sequence of seven …
uptake of scarce nutrients. In TonB-dependent transporters, a conserved sequence of seven …
Structures of human bile acid exporter ABCB11 reveal a transport mechanism facilitated by two tandem substrate-binding pockets
Dear Editor, Bile acids are a group of cholesterol-derived physiological surfactants required
for digestion of lipids and fat-soluble vitamins. 1 However, excess of bile acids is detrimental …
for digestion of lipids and fat-soluble vitamins. 1 However, excess of bile acids is detrimental …
[HTML][HTML] Translocation of the ABC transporter ABCD4 from the endoplasmic reticulum to lysosomes requires the escort protein LMBD1
K Kawaguchi, T Okamoto, M Morita, T Imanaka - Scientific reports, 2016 - nature.com
We previously demonstrated that ABCD4 does not localize to peroxisomes but rather, the
endoplasmic reticulum (ER), because it lacks the NH2-terminal hydrophilic region required …
endoplasmic reticulum (ER), because it lacks the NH2-terminal hydrophilic region required …
In meso structure of the cobalamin transporter, BtuB, at 1.95 Å resolution
Crystals of the apo form of the vitamin B12 and colicin receptor, BtuB, that diffract to 1.95 Å
have been grown by the membrane-based in meso technique. The structure of the protein …
have been grown by the membrane-based in meso technique. The structure of the protein …
Structures of the nucleotide-binding domain of the human ABCB6 transporter and its complexes with nucleotides
M Haffke, A Menzel, Y Carius, D Jahn… - … Section D: Biological …, 2010 - scripts.iucr.org
The human ATP-binding cassette (ABC) transporter ABCB6 is involved in haem-precursor
transport across the mitochondrial membrane. The crystal structure of its nucleotide-binding …
transport across the mitochondrial membrane. The crystal structure of its nucleotide-binding …