1MJY

STRUCTURE OF INORGANIC PYROPHOSPHATASE MUTANT D70N

Summary for 1MJY

• Entry DOI: 10.2210/pdb1mjy/pdb
• Descriptor: INORGANIC PYROPHOSPHATASE (2 entities in total)
• Functional Keywords: hydrolase, acid anhydride hydrolase, mutation
• Biological source: Escherichia coli
• Cellular location: Cytoplasm: P0A7A9
• Total number of polymer chains: 2
• Total formula weight: 39168.59

Authors

Oganesyan, V.,Harutyunyan, E.H.,Avaeva, S.M.,Huber, R. (deposition date: 1997-02-08, release date: 1997-12-03, Last modification date: 2024-02-14)

Primary citation

Avaeva, S.M.,Rodina, E.V.,Vorobyeva, N.N.,Kurilova, S.A.,Nazarova, T.I.,Sklyankina, V.A.,Oganessyan, V.Y.,Samygina, V.R.,Harutyunyan, E.H.
Three-dimensional structures of mutant forms of E. coli inorganic pyrophosphatase with Asp-->Asn single substitution in positions 42, 65, 70, and 97.
Biochemistry Mosc., 63:671-684, 1998

PubMed Abstract: The three-dimensional structures of four mutant E. coli inorganic pyrophosphatases (PPases) with single Asp-->Asn substitutions at positions 42, 65, 70, and 97 were solved at 1.95, 2.15, 2.10, and 2.20 A resolution, respectively. Asp-42-->Asn and Asp-65-->Asn mutant PPases were prepared as complexes with sulfate--a structural analog of phosphate, the product of enzymatic reaction. A comparison of mutant enzymes with native PPases revealed that a single amino acid substitution changes the position of the mutated residue as well as the positions of several functional groups and some parts of a polypeptide chain. These changes are responsible for the fact that mutant PPases differ from the native ones in their catalytic properties. The sulfate binding to the mutant PPase active site causes molecular asymmetry, as shown for the native PPase earlier. The subunit asymmetry is manifested in different positions of sulfate and several functional groups, as well as changes in packing of hexamers in crystals and in cell parameters.

PubMed: 9668207

Experimental method

X-RAY DIFFRACTION (2.1 Å)