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PDB ID 1faj

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1faj, resolution 2.15Å ()
Activity: Inorganic diphosphatase, with EC number 3.6.1.1
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml


Soluble inorganic pyrophosphatase is a ubiquitous enzyme that plays an important role in energy metabolism [1]. Energy metabolism is made possible by soluble inorganic pyrophosphatases (PPases) by their hydrolyzing inorganic phosphates into two molecules of orthophosphate [2]. PPases may have had an important role in evolution by aiding in accurate DNA copying during chromosome duplication [1]. Escherichia coli (E-coli bacteria) and Saccharomyces cerevisiae (S. cerevisiae yeast) PPases, E-PPase and Y-PPase respectively, are the two best studied PPases [1].

Inorganic Pyrophosphatase

Contents


Structure

E-PPase, a homohexameric protein [3], contains 175 amino-acid residues in each subunit [4].

Function

References

  1. ↑ 1.0 1.1 1.2 Kankare J, Neal GS, Salminen T, Glumoff T, Glumhoff T [corrected to Glumoff T, Cooperman BS, Lahti R, Goldman A. The structure of E.coli soluble inorganic pyrophosphatase at 2.7 A resolution. Protein Eng. 1994 Jul;7(7):823-30. PMID:7971944
  2. ↑ Samygina VR, Popov AN, Rodina EV, Vorobyeva NN, Lamzin VS, Polyakov KM, Kurilova SA, Nazarova TI, Avaeva SM. The structures of Escherichia coli inorganic pyrophosphatase complexed with Ca(2+) or CaPP(i) at atomic resolution and their mechanistic implications. J Mol Biol. 2001 Nov 30;314(3):633-45. PMID:11846572 doi:10.1006/jmbi.2001.5149
  3. ↑ Wong SC, Burton PM, Josse J. Constitutive inorganic pyrophosphatase of Escherichia coli. V. Reconstitution of native enzyme particles from subunit polypeptide chains. J Biol Chem. 1970 Sep 10;245(17):4353-7. PMID:5498422
  4. ↑ Lahti R, Pitkaranta T, Valve E, Ilta I, Kukko-Kalske E, Heinonen J. Cloning and characterization of the gene encoding inorganic pyrophosphatase of Escherichia coli K-12. J Bacteriol. 1988 Dec;170(12):5901-7. PMID:2848015
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