1ii0
From Proteopedia
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|PDB= 1ii0 |SIZE=350|CAPTION= <scene name='initialview01'>1ii0</scene>, resolution 2.40Å | |PDB= 1ii0 |SIZE=350|CAPTION= <scene name='initialview01'>1ii0</scene>, resolution 2.40Å | ||
|SITE= | |SITE= | ||
- | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=ATP:ADENOSINE-5'-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TAS:TRIHYDROXYARSENITE(III)'>TAS</scene> |
- | |ACTIVITY= [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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= ARSA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |GENE= ARSA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
+ | |DOMAIN= | ||
+ | |RELATEDENTRY=[[1f48|1F48]], [[1ihu|1IHU]], [[1ii9|1II9]] | ||
+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ii0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ii0 OCA], [http://www.ebi.ac.uk/pdbsum/1ii0 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ii0 RCSB]</span> | ||
}} | }} | ||
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[[Category: Rosen, B P.]] | [[Category: Rosen, B P.]] | ||
[[Category: Zhou, T.]] | [[Category: Zhou, T.]] | ||
- | [[Category: ADP]] | ||
- | [[Category: ATP]] | ||
- | [[Category: CD]] | ||
- | [[Category: CL]] | ||
- | [[Category: MG]] | ||
- | [[Category: TAS]] | ||
[[Category: arsa atpase]] | [[Category: arsa atpase]] | ||
[[Category: atp]] | [[Category: atp]] | ||
- | [[Category: atp binding site]] | + | [[Category: atp binding site,]] |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:20:01 2008'' |
Revision as of 18:20, 30 March 2008
| |||||||
, resolution 2.40Å | |||||||
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Ligands: | , , , , , | ||||||
Gene: | ARSA (Escherichia coli) | ||||||
Activity: | Arsenite-transporting ATPase, with EC number 3.6.3.16 | ||||||
Related: | 1F48, 1IHU, 1II9
| ||||||
Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
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. 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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