1ii9: Difference between revisions

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[[Image:1ii9.gif|left|200px]]
{{Seed}}
[[Image:1ii9.png|left|200px]]


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{{STRUCTURE_1ii9|  PDB=1ii9  |  SCENE=  }}  
{{STRUCTURE_1ii9|  PDB=1ii9  |  SCENE=  }}  


'''CRYSTAL STRUCTURE OF THE ESCHERICHIA COLI ARSENITE-TRANSLOCATING ATPASE IN COMPLEX WITH AMP-PNP'''
===CRYSTAL STRUCTURE OF THE ESCHERICHIA COLI ARSENITE-TRANSLOCATING ATPASE IN COMPLEX WITH AMP-PNP===




==Overview==
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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.
The line below this paragraph, {{ABSTRACT_PUBMED_11395509}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_11395509}}


==About this Structure==
==About this Structure==
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[[Category: Arsa atpase]]
[[Category: Arsa atpase]]
[[Category: Atp binding site]]
[[Category: Atp binding site]]
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