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Structures of the nucleotide-binding domain of the human ABCB6 transporter and its complexes with nucleotides.
Haffke, Matthias Menzel, Anja Carius, Yvonne Jahn, Dieter Heinz, Dirk W
Haffke, Matthias
Menzel, Anja
Carius, Yvonne
Jahn, Dieter
Heinz, Dirk W
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2010-09
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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.
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Structures of the nucleotide-binding domain of the human ABCB6 transporter and its complexes with nucleotides. 2010, 66 (Pt 9):979-87 Acta Crystallogr. D Biol. Crystallogr.
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en
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1399-0047