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Structure paper

TitleConformational changes in four regions of the Escherichia coli ArsA ATPase link ATP hydrolysis to ion translocation.
Journal, issue, pagesJ. Biol. Chem., Vol. 276, Page 30414-30422, Year 2001
Publish dateApr 20, 2001 (structure data deposition date)
AuthorsZhou, T. / Radaev, S. / Rosen, B.P. / Gatti, D.L.
External linksJ. Biol. Chem. / PubMed:11395509
MethodsX-ray diffraction
Resolution2.15 - 2.6 Å
Structure data

PDB-1ihu:
CRYSTAL STRUCTURE OF THE ESCHERICHIA COLI ARSENITE-TRANSLOCATING ATPASE IN COMPLEX WITH MG-ADP-ALF3
Method: X-RAY DIFFRACTION / Resolution: 2.15 Å

PDB-1ii0:
CRYSTAL STRUCTURE OF THE ESCHERICHIA COLI ARSENITE-TRANSLOCATING ATPASE
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

PDB-1ii9:
CRYSTAL STRUCTURE OF THE ESCHERICHIA COLI ARSENITE-TRANSLOCATING ATPASE IN COMPLEX WITH AMP-PNP
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-CD:
Unknown entry

ChemComp-CL:
Unknown entry

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

ChemComp-AF3:
ALUMINUM FLUORIDE

ChemComp-TAS:
TRIHYDROXYARSENITE(III)

ChemComp-HOH:
WATER

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

ChemComp-ANP:
PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / AMP-PNP, energy-carrying molecule analogue*YM

Source
  • escherichia coli (E. coli)
KeywordsHYDROLASE / Aluminum Fluoride / ADP / ArsA ATPase / ATP binding site / AMP-PNP

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