1f48

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spinqualitylabelsall models 1f48, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

CRYSTAL STRUCTURE OF THE ESCHERICHIA COLI ARSENITE-TRANSLOCATING ATPASE

Overview

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.

About this Structure

1F48 is a Single protein structure of sequence from Escherichia coli with SB, MG, CD, CL, SBO and ADP as ligands. Full crystallographic information is available from OCA.

Reference

Structure of the ArsA ATPase: the catalytic subunit of a heavy metal resistance pump., Zhou T, Radaev S, Rosen BP, Gatti DL, EMBO J. 2000 Sep 1;19(17):4838-45. PMID:10970874

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