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Acta Crystallogr D Biol Crystallogr. 2010 Sep;66(Pt 9):979-87. doi: 10.1107/S0907444910028593. Epub 2010 Aug 13.

Structures of the nucleotide-binding domain of the human ABCB6 transporter and its complexes with nucleotides.

Author information

1
Helmholtz Zentrum für Infektionsforschung, Braunschweig, Germany.

Abstract

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 domain (NBD) has been determined in the apo form and in complexes with ADP, with ADP and Mg(2+) and with ATP at high resolution. The overall structure is L-shaped and consists of two lobes, consistent with other reported NBD structures. Nucleotide binding is mediated by the highly conserved Tyr599 and the Walker A motif, and induces notable structural changes. Structural comparison with other structurally characterized NBDs and full-length ABC transporters gives the first insight into the possible catalytic mechanism of ABCB6 and the role of the N-terminal helix alpha(1) in full-length ABCB6.

PMID:
20823549
DOI:
10.1107/S0907444910028593
[Indexed for MEDLINE]

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