PDBsum entry 4mrr

Transport protein

PDB id: 4mrr

Contents

Protein chains

600 a.a.

Ligands

LDA ×4

MSE ×2

PO4 ×6

PDB id:

4mrr

Name:

Transport protein

Title:

Structure of a bacterial atm1-family abc transporter

Structure:

Abc transporter related protein. Chain: a, b. Engineered: yes

Source:

Novosphingobium aromaticivorans. Organism_taxid: 279238. Strain: dsm 12444. Gene: atm1, saro_2631. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.97Å R-factor: 0.205 R-free: 0.236

Authors:

J.Y.Lee,J.G.Yang,D.Zhitnitsky,O.Lewinson,D.C.Rees

Key ref:

J.Y.Lee et al. (2014). Structural basis for heavy metal detoxification by an Atm1-type ABC exporter. Science, 343, 1133-1136. PubMed id: 24604198 DOI: 10.1126/science.1246489

Date:

17-Sep-13 Release date: 19-Mar-14

Protein chains

Q2G506  (ATM1_NOVAD) -  ATM1-type heavy metal exporter from Novosphingobium aromaticivorans (strain ATCC 700278 / DSM 12444 / CCUG 56034 / CIP 105152 / NBRC 16084 / F199)

Seq: 608 a.a.

Struc: 600 a.a.

Enzyme reactions

• Enzyme class: E.C.7.-.-.-

DOI no: 10.1126/science.1246489

Science 343:1133-1136 (2014)

PubMed id: 24604198

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

J.Y.Lee, J.G.Yang, D.Zhitnitsky, O.Lewinson, D.C.Rees.

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.