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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Structures of the nucleotide-binding domain of the human ABCB6 transporter and its complexes with nucleotides.
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Structures of the nucleotide-binding domain of the human ABCB6 transporter and its complexes with nucleotides.

机译：结构的nucleotide-binding域人类ABCB6运输车及其复合物核苷酸。

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摘要

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.
机译：人类的磷酸腺苷磁带(ABC)运输车ABCB6参与haem-precursor运输在线粒体膜。结构的nucleotide-binding域(NBD)已经决定在人群的形式和在吗复合物ADP, ADP和镁(2 +)在高分辨率的ATP。l型,由两个叶,一致与其他报道NBD结构。绑定是由高度保守的Tyr599和沃克主题,诱发显著的结构性变化。与其他结构nbd和特点完整的ABC转运蛋白给第一了解可能的催化机理ABCB6和氨基端螺旋的角色在长篇ABCB6α(1)。

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