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The structure of E.coli soluble inorganic pyrophosphatase has been refined at 2.7 A resolution to an R-factor of 20.9%. The overall fold of the molecule is essentially the same as yeast pyrophosphatase, except that yeast pyrophosphatase is longer at both the N- and C-termini. Escherichia coli pyrophosphatase is a mixed alpha + beta protein with a complicated topology. The active site cavity, which is also very similar to the yeast enzyme, is formed by seven beta-strands and an alpha-helix and has a rather asymmetric distribution of charged residues. Our structure-based alignment extends and improves upon earlier sequence alignment studies; it shows that probably no more than 14, not 15-17 charged and polar residues are part of the conserved enzyme mechanism of pyrophosphatases. Six of these conserved residues, at the bottom of the active site cavity, form a tight group centred on Asp70 and probably bind the two essential Mg2+ ions. The others, more spreadout and more positively charged, presumably bind substrate. Escherichia coli pyrophosphatase has an extra aspartate residue in the active site cavity, which may explain why the two enzymes bind divalent cation differently. Based on the structure, we have identified a sequence motif that seems to occur only in soluble inorganic pyrophosphatases.
J Kankare, and
G S Neal, and
T Salminen, and
T Glumoff, and
T ] Glumhoff T [corrected to Glumoff, and
B S Cooperman, and
R Lahti, and
A Goldman
May 1996,
Acta crystallographica. Section D, Biological crystallography,
J Kankare, and
G S Neal, and
T Salminen, and
T Glumoff, and
T ] Glumhoff T [corrected to Glumoff, and
B S Cooperman, and
R Lahti, and
A Goldman
August 2011,
Acta crystallographica. Section F, Structural biology and crystallization communications,
J Kankare, and
G S Neal, and
T Salminen, and
T Glumoff, and
T ] Glumhoff T [corrected to Glumoff, and
B S Cooperman, and
R Lahti, and
A Goldman
June 2007,
Acta crystallographica. Section D, Biological crystallography,
J Kankare, and
G S Neal, and
T Salminen, and
T Glumoff, and
T ] Glumhoff T [corrected to Glumoff, and
B S Cooperman, and
R Lahti, and
A Goldman
January 1980,
Journal of molecular biology,
J Kankare, and
G S Neal, and
T Salminen, and
T Glumoff, and
T ] Glumhoff T [corrected to Glumoff, and
B S Cooperman, and
R Lahti, and
A Goldman
September 1990,
Proceedings of the National Academy of Sciences of the United States of America,
J Kankare, and
G S Neal, and
T Salminen, and
T Glumoff, and
T ] Glumhoff T [corrected to Glumoff, and
B S Cooperman, and
R Lahti, and
A Goldman
March 1990,
Biochemistry,
J Kankare, and
G S Neal, and
T Salminen, and
T Glumoff, and
T ] Glumhoff T [corrected to Glumoff, and
B S Cooperman, and
R Lahti, and
A Goldman
October 2001,
Biochemistry,
J Kankare, and
G S Neal, and
T Salminen, and
T Glumoff, and
T ] Glumhoff T [corrected to Glumoff, and
B S Cooperman, and
R Lahti, and
A Goldman
December 1991,
Journal of biochemistry,
J Kankare, and
G S Neal, and
T Salminen, and
T Glumoff, and
T ] Glumhoff T [corrected to Glumoff, and
B S Cooperman, and
R Lahti, and
A Goldman
June 1997,
Biochemistry,
J Kankare, and
G S Neal, and
T Salminen, and
T Glumoff, and
T ] Glumhoff T [corrected to Glumoff, and
B S Cooperman, and
R Lahti, and
A Goldman
June 2003,
Virology,
