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

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 Mg2+ and with ATP at high resolut...

Full description

Saved in:
Bibliographic Details
Published in:Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 2010-09, Vol.66 (9), p.979-987
Main Authors: Haffke, Matthias, Menzel, Anja, Carius, Yvonne, Jahn, Dieter, Heinz, Dirk W.
Format: Article
Language:English
Subjects:
ABC transporters
ABCB6
Amino Acid Sequence
Animals
ATP-Binding Cassette Transporters - chemistry
Crystallography, X-Ray
haem biosynthesis
Humans
Models, Molecular
Molecular Sequence Data
nucleotide-binding domains
Nucleotides - chemistry
Protein Interaction Domains and Motifs
Protein Structure, Tertiary
Sequence Alignment
Structural Homology, Protein
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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 Mg2+ 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 α1 in full‐length ABCB6.
ISSN:1399-0047
0907-4449
1399-0047
DOI:10.1107/S0907444910028593