1INO

RECOMBINANT INORGANIC PYROPHOSPHATASE FROM ESCHERICHIA COLI

Summary for 1INO

• Entry DOI: 10.2210/pdb1ino/pdb
• Descriptor: INORGANIC PYROPHOSPHATASE, MANGANESE (II) ION (3 entities in total)
• Functional Keywords: metal binding, mn2+ ion, complex, acid anhydride hydrolase
• Biological source: Escherichia coli
• Cellular location: Cytoplasm: P0A7A9
• Total number of polymer chains: 1
• Total formula weight: 19652.27

Authors

Oganesyan, V.Yu.,Avaeva, S.M.,Harutyunyan, E.H. (deposition date: 1995-10-03, release date: 1996-04-03, Last modification date: 2024-02-07)

Primary citation

Avaeva, S.M.,Rodina, E.V.,Kurilova, S.A.,Nazarova, T.I.,Vorobyeva, N.N.,Harutyunyan, E.H.,VYu, Oganessyan
Mg2+ activation of Escherichia coli inorganic pyrophosphatase.
Febs Lett., 377:44-46, 1995

PubMed Abstract: Further refinement of X-ray data on Escherichia coli inorganic pyrophosphatase [Oganessyan et al. (1994) FEBS Lett. 348, 301-304] to 2.2 A reveals a system of noncovalent interactions involving Tyr55 and Tyr141 in the active site. The pKa for one of the eight Tyr residues in wild-type pyrophosphatase is as low as 9.1 and further decreases to 8.1 upon Mg2+ binding, generating characteristic changes in the absorption spectrum. These effects are lost in a Y55F but not in a Y141F variant. It is suggested that the lower-affinity site for Mg2+ in the enzyme is formed by Tyr55 and Asp70, which are in close proximity in the apo-enzyme structure.

PubMed: 8543015
DOI: 10.1016/0014-5793(95)01310-5

Experimental method

X-RAY DIFFRACTION (2.2 Å)