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Structure paper

TitleStructural and kinetic analyses of arginine residues in the active site of the acetate kinase from Methanosarcina thermophila.
Journal, issue, pagesJ. Biol. Chem., Vol. 280, Page 10731-10742, Year 2005
Publish dateJun 25, 2004 (structure data deposition date)
AuthorsGorrell, A. / Lawrence, S.H. / Ferry, J.G.
External linksJ. Biol. Chem. / PubMed:15647264
MethodsX-ray diffraction
Resolution2.5 - 3 Å
Structure data

PDB-1tuu:
Acetate Kinase crystallized with ATPgS
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

PDB-1tuy:
Acetate Kinase complexed with ADP, AlF3 and acetate
Method: X-RAY DIFFRACTION / Resolution: 3 Å

Chemicals

ChemComp-SO4:
SULFATE ION

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

ChemComp-NH4:
AMMONIUM ION

ChemComp-AMP:
ADENOSINE MONOPHOSPHATE / AMP*YM

ChemComp-PIS:
TRIHYDROGEN THIODIPHOSPHATE

ChemComp-HOH:
WATER

ChemComp-AF3:
ALUMINUM FLUORIDE

ChemComp-ACY:
ACETIC ACID

Source
  • methanosarcina thermophila (archaea)
KeywordsTRANSFERASE / alpha/beta / ASKHA (acetate and sugar kinases / HSC70 Actin) superfamily / two similar domains / hsc70 / actin) superfamily / AlF3 and acetate

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