4MRN: Structure Of A Bacterial Atm1-family Abc Transporter

Citation:
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.
PDB ID: 4MRNDownload
MMDB ID: 118446
PDB Deposition Date: 2013/9/17
Updated in MMDB: 2014/03
Experimental Method:
x-ray diffraction
Resolution: 2.5  Å
Source Organism:
Similar Structures:
Biological Unit for 4MRN: dimeric; determined by author and by software (PISA)
Molecular Components in 4MRN
Label Count Molecule
Proteins (2 molecules)
2
ABC Transporter Related Protein
Molecule annotation
Chemicals (10 molecules)
1
4
2
6
* Click molecule labels to explore molecular sequence information.

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