Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 2019 Dec;29(12):1039-1041.
doi: 10.1038/s41422-019-0222-z. Epub 2019 Aug 29.

Cryo-EM structure of human lysosomal cobalamin exporter ABCD4

Da Xu #  1 , Zhang Feng #  1 , Wen-Tao Hou  1 , Yong-Liang Jiang  1 , Liang Wang  1 , Linfeng Sun  2   3 , Cong-Zhao Zhou  4 , Yuxing Chen  5
Affiliations

Cryo-EM structure of human lysosomal cobalamin exporter ABCD4

Da Xu et al. Cell Res. 2019 Dec.
No abstract available

PubMed Disclaimer

Conflict of interest statement

The authors declare no competing interests.

Figures

Fig. 1
Fig. 1
Cryo-EM structure of human lysosomal cobalamin exporter ABCD4. a The structure of ABCD4 in a lysosome-open state is shown in two perpendicular views with cartoon representation. The two monomers are colored in violet and blue, respectively. ATP molecule is shown in sticks and colored by elements. b A top view of ABCD4 from the inside of lysosome. The six TM helices of each monomer are indicated by numbers. c The NBD of ABCD4 adopts a head-to-tail state with ATP sandwiched between Walker A motif of one NBD and ABC signature motif of the other. The NBD is colored in light gray. The Walker A motif and ABC signature motif of each monomer are colored in violet and blue, respectively. ATP is shown as sticks. d ATP-binding pattern of ABCD4. Residues at the ATP-binding site are shown as sticks. Hydrogen bonds and ionic interactions between ABCD4 and ATP are indicated by dash lines. e Superposition of ATP-binding sites of ABCB1(PDB code: 6C0V) and ABCD4. Pro526 and Gly1178 in the signature motifs of ABCD4 and ABCB1, are shown as sticks, respectively. The ABCB1 and ATP molecule in ABCB1 are both colored in light gray. f Multiple-sequence alignment of the signature motifs. Sequences include human ABCD4 and homologs from Mus musculus, Canis familiaris, Brachydanio rerio, and Caenorhabditis elegans, and the putative cobalamin transporter Rv1819c in Mycobacterium tuberculosis, as well as human ABCB1, ABCC7, and ABCG2, Sav1866 in Staphylococcus aureus, and the E. coli MsbA, MalK, and BtuD. g A section view for the electrostatic surface potential of the substrate cavity in ABCD4, colored by electrostatic potential ranging from blue (most positive) to red (most negative). h Residues at the substrate cavity shown as sticks. i Mapping of three clinically identified pathogenic mutations, N141K, F319C, and R432Q to ABCD4 structure. The Cα atoms of the indicated residues are shown as spheres. Close-up views of the local structure around Tyr319, Asn141, and Arg432 are shown on right
See this image and copyright information in PMC

Similar articles

See all similar articles

Cited by

See all "Cited by" articles

References

    1. Watanabe F. Exp. Biol. Med. 2007;232:1266–1274. doi: 10.3181/0703-MR-67. - DOI - PubMed
    1. Nielsen, M. J., Rasmussen, M. R., Andersen, C. B., Nexø, E. & Moestrup, S. K. Nat. Rev. Gastroenterol. Hepatol. 9, 345–354 (2012). - PubMed
    1. Coelho D, et al. Nat. Genet. 2012;44:1152–1155. doi: 10.1038/ng.2386. - DOI - PubMed
    1. Dean M, Hamon Y, Chimini G. J. Lipid Res. 2001;42:1007–1017. - PubMed
    1. Okamoto T, et al. Biochem. Biophys. Res. Commun. 2018;496:1122–1127. doi: 10.1016/j.bbrc.2018.01.153. - DOI - PubMed

LinkOut - more resources