4MRN

Structure of a bacterial Atm1-family ABC transporter

Summary for 4MRN

• Entry DOI: 10.2210/pdb4mrn/pdb
• Related: 4MRP 4MRR 4MRS 4MRV
• Descriptor: ABC transporter related protein, LAURYL DIMETHYLAMINE-N-OXIDE, PHOSPHATE ION, ... (4 entities in total)
• Functional Keywords: membrane protein, substrate exporter, heavy metal resistance, membrane, transport protein
• Biological source: Novosphingobium aromaticivorans
• Total number of polymer chains: 2
• Total formula weight: 138249.92

Authors

Lee, J.Y.,Yang, J.G.,Zhitnitsky, D.,Lewinson, O.,Rees, D.C. (deposition date: 2013-09-17, release date: 2014-03-19, Last modification date: 2024-11-20)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.5 Å)