Unknown

Dataset Information

0

Structural basis for heavy metal detoxification by an Atm1-type ABC exporter.


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.

SUBMITTER: Lee JY 

PROVIDER: S-EPMC4151877 | biostudies-literature | 2014 Mar

REPOSITORIES: biostudies-literature

altmetric image

Publications

Structural basis for heavy metal detoxification by an Atm1-type ABC exporter.

Lee Jonas Y JY   Yang Janet G JG   Zhitnitsky Daniel D   Lewinson Oded O   Rees Douglas C DC  

Science (New York, N.Y.) 20140301 6175


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. Consisten  ...[more]

Similar Datasets

| S-EPMC4121816 | biostudies-literature
| S-EPMC7430982 | biostudies-literature
| S-EPMC3654245 | biostudies-other
2017-01-01 | GSE83445 | GEO
| S-EPMC4617439 | biostudies-literature
| PRJEB22938 | ENA
| S-EPMC6222291 | biostudies-literature
| S-EPMC5540610 | biostudies-literature
| S-EPMC8694623 | biostudies-literature
2021-10-02 | GSE163156 | GEO