1ii0
From Proteopedia
(New page: 200px<br /><applet load="1ii0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ii0, resolution 2.40Å" /> '''CRYSTAL STRUCTURE OF...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1ii0.gif|left|200px]]<br /><applet load="1ii0" size=" | + | [[Image:1ii0.gif|left|200px]]<br /><applet load="1ii0" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ii0, resolution 2.40Å" /> | caption="1ii0, resolution 2.40Å" /> | ||
'''CRYSTAL STRUCTURE OF THE ESCHERICHIA COLI ARSENITE-TRANSLOCATING ATPASE'''<br /> | '''CRYSTAL STRUCTURE OF THE ESCHERICHIA COLI ARSENITE-TRANSLOCATING ATPASE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Structures of ArsA with ATP, AMP-PNP, or ADP.AlF(3) bound at the A2 | + | 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== | ==About this Structure== | ||
| - | 1II0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with CD, CL, MG, ADP, ATP and TAS as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Arsenite-transporting_ATPase Arsenite-transporting ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.16 3.6.3.16] Full crystallographic information is available from [http:// | + | 1II0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=CD:'>CD</scene>, <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=ADP:'>ADP</scene>, <scene name='pdbligand=ATP:'>ATP</scene> and <scene name='pdbligand=TAS:'>TAS</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Arsenite-transporting_ATPase Arsenite-transporting ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.16 3.6.3.16] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1II0 OCA]. |
==Reference== | ==Reference== | ||
| Line 14: | Line 14: | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Gatti, D | + | [[Category: Gatti, D L.]] |
[[Category: Radaev, S.]] | [[Category: Radaev, S.]] | ||
| - | [[Category: Rosen, B | + | [[Category: Rosen, B P.]] |
[[Category: Zhou, T.]] | [[Category: Zhou, T.]] | ||
[[Category: ADP]] | [[Category: ADP]] | ||
| Line 28: | Line 28: | ||
[[Category: atp binding site]] | [[Category: atp binding site]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:12:03 2008'' |
Revision as of 11:12, 21 February 2008
|
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 , , , , and 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
Page seeded by OCA on Thu Feb 21 13:12:03 2008
Categories: Arsenite-transporting ATPase | Escherichia coli | Single protein | Gatti, D L. | Radaev, S. | Rosen, B P. | Zhou, T. | ADP | ATP | CD | CL | MG | TAS | Arsa atpase | Atp | Atp binding site
