3NH9

Nucleotide Binding Domain of Human ABCB6 (ATP bound structure)

Summary for 3NH9

• Entry DOI: 10.2210/pdb3nh9/pdb
• Related: 3NH6 3NHA 3NHB
• Descriptor: ATP-binding cassette sub-family B member 6, mitochondrial, ADENOSINE-5'-TRIPHOSPHATE, BETA-MERCAPTOETHANOL, ... (4 entities in total)
• Functional Keywords: abc-transporter, abcb6, nucleotide binding domain, heme biosynthesis, transport protein
• Biological source: Homo sapiens (human)
• Cellular location: Mitochondrion outer membrane; Multi-pass membrane protein: Q9NP58
• Total number of polymer chains: 1
• Total formula weight: 34151.21

Authors

Haffke, M.,Menzel, A.,Carius, Y.,Jahn, D.,Heinz, D.W. (deposition date: 2010-06-14, release date: 2010-08-25, Last modification date: 2023-09-06)

Primary citation

Haffke, M.,Menzel, A.,Carius, Y.,Jahn, D.,Heinz, D.W.
Structures of the nucleotide-binding domain of the human ABCB6 transporter and its complexes with nucleotides.
Acta Crystallogr.,Sect.D, 66:979-987, 2010

PubMed 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.

PubMed: 20823549
DOI: 10.1107/S0907444910028593

Experimental method

X-RAY DIFFRACTION (2.1 Å)