4mrs

Structure of a bacterial Atm1-family ABC transporter

spinqualitylabelsall models 4mrs, resolution 2.35Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4mrs is a 2 chain structure with sequence from Novosphingobium aromaticivorans DSM 12444. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.35Å Ligands: GDS, LDA, MSE, PO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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. Structural basis for heavy metal detoxification by an Atm1-type ABC exporter.,Lee JY, Yang JG, Zhitnitsky D, Lewinson O, Rees DC Science. 2014 Mar 7;343(6175):1133-6. doi: 10.1126/science.1246489. PMID:24604198 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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