1F48

CRYSTAL STRUCTURE OF THE ESCHERICHIA COLI ARSENITE-TRANSLOCATING ATPASE

Summary for 1F48

• Entry DOI: 10.2210/pdb1f48/pdb
• Descriptor: ARSENITE-TRANSLOCATING ATPASE, ANTIMONY (III) ION, MAGNESIUM ION, ... (8 entities in total)
• Functional Keywords: p-loop, antimonite binding site, atp binding site, hydrolase
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 66306.89

Authors

Zhou, T.,Radaev, S.,Rosen, B.P.,Gatti, D.L. (deposition date: 2000-06-07, release date: 2000-09-13, Last modification date: 2024-02-07)

Primary citation

Zhou, T.,Radaev, S.,Rosen, B.P.,Gatti, D.L.
Structure of the ArsA ATPase: the catalytic subunit of a heavy metal resistance pump.
EMBO J., 19:4838-4845, 2000

PubMed Abstract: Active extrusion is a common mechanism underlying detoxification of heavy metals, drugs and antibiotics in bacteria, protozoa and mammals. In Escherichia coli, the ArsAB pump provides resistance to arsenite and antimonite. This pump consists of a soluble ATPase (ArsA) and a membrane channel (ArsB). ArsA contains two nucleotide-binding sites (NBSs) and a binding site for arsenic or antimony. Binding of metalloids stimulates ATPase activity. The crystal structure of ArsA reveals that both NBSs and the metal-binding site are located at the interface between two homologous domains. A short stretch of residues connecting the metal-binding site to the NBSs provides a signal transduction pathway that conveys information on metal occupancy to the ATP hydrolysis sites. Based on these structural features, we propose that the metal-binding site is involved directly in the process of vectorial translocation of arsenite or antimonite across the membrane. The relative positions of the NBS and the inferred mechanism of allosteric activation of ArsA provide a useful model for the interaction of the catalytic domains in other transport ATPases.

PubMed: 10970874
DOI: 10.1093/emboj/19.17.4838

Experimental method

X-RAY DIFFRACTION (2.3 Å)