4MRN

Structure of a bacterial Atm1-family ABC transporter

4MRN の概要

• エントリーDOI: 10.2210/pdb4mrn/pdb
• 関連するPDBエントリー: 4MRP 4MRR 4MRS 4MRV
• 分子名称: ABC transporter related protein, LAURYL DIMETHYLAMINE-N-OXIDE, PHOSPHATE ION, ... (4 entities in total)
• 機能のキーワード: membrane protein, substrate exporter, heavy metal resistance, membrane, transport protein
• 由来する生物種: Novosphingobium aromaticivorans
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 138249.92

構造登録者

Lee, J.Y.,Yang, J.G.,Zhitnitsky, D.,Lewinson, O.,Rees, D.C. (登録日: 2013-09-17, 公開日: 2014-03-19, 最終更新日: 2024-11-20)

主引用文献

Lee, J.Y.,Yang, J.G.,Zhitnitsky, D.,Lewinson, O.,Rees, D.C.
Structural basis for heavy metal detoxification by an Atm1-type ABC exporter.
Science, 343:1133-1136, 2014

PubMed Abstract: Although substantial progress has been achieved in the structural analysis of exporters from the superfamily of adenosine triphosphate (ATP)-binding cassette (ABC) transporters, much less is known about how they selectively recognize substrates and how substrate binding is coupled to ATP hydrolysis. We have addressed these questions through crystallographic analysis of the Atm1/ABCB7/HMT1/ABCB6 ortholog from Novosphingobium aromaticivorans DSM 12444, NaAtm1, at 2.4 angstrom resolution. Consistent with a physiological role in cellular detoxification processes, functional studies showed that glutathione derivatives can serve as substrates for NaAtm1 and that its overexpression in Escherichia coli confers protection against silver and mercury toxicity. The glutathione binding site highlights the articulated design of ABC exporters, with ligands and nucleotides spanning structurally conserved elements to create adaptable interfaces accommodating conformational rearrangements during the transport cycle.

PubMed: 24604198
DOI: 10.1126/science.1246489

実験手法

X-RAY DIFFRACTION (2.5 Å)