1ii0

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spinqualitylabelsall models 1ii0, resolution 2.40Å 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

Structures of ArsA with ATP, AMP-PNP, or ADP.AlF(3) bound at the A2, nucleotide binding site were determined. Binding of different nucleotides, modifies the coordination sphere of Mg(2+). In particular, the changes, elicited by ADP.AlF(3) provide insights into the mechanism of ATP, hydrolysis. In-line attack by water onto the gamma-phosphate of ATP would, be followed first by formation of a trigonal intermediate and then by, breaking of the scissile bond between the beta- and gamma-phosphates., Motions of amino acid side chains at the A2 nucleotide binding site during, ATP binding and hydrolysis propagate at a distance, producing, conformational changes in four different regions of the protein, corresponding to helices H4-H5, helices H9-H10, helices H13-H15, and to, the S1-H2-S2 region. These elements are extensions of, respectively, the, Switch I and Switch II regions, the A-loop (a small loop near the, nucleotide adenine moiety), and the P-loop. Based on the observed, conformational changes, it is proposed that ArsA functions as a, reciprocating engine that hydrolyzes 2 mol of ATP per each cycle of ion, translocation across the membrane.

About this Structure

1II0 is a Single protein structure of sequence from Escherichia coli with CD, CL, MG, ADP, ATP and TAS as ligands. Active as Arsenite-transporting ATPase, with EC number 3.6.3.16 Full crystallographic information is available from OCA.

Reference

Conformational changes in four regions of the Escherichia coli ArsA ATPase link ATP hydrolysis to ion translocation., Zhou T, Radaev S, Rosen BP, Gatti DL, J Biol Chem. 2001 Aug 10;276(32):30414-22. Epub 2001 Jun 6. PMID:11395509

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