1MJW

STRUCTURE OF INORGANIC PYROPHOSPHATASE MUTANT D42N

1MJW の概要

• エントリーDOI: 10.2210/pdb1mjw/pdb
• 分子名称: INORGANIC PYROPHOSPHATASE, SULFATE ION (3 entities in total)
• 機能のキーワード: hydrolase, acid anhydride hydrolase, mutation
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cytoplasm: P0A7A9
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 39384.82

構造登録者

Oganesyan, V.,Harutyunyan, E.H.,Avaeva, S.M.,Samygina, V.R.,Huber, R. (登録日: 1997-02-08, 公開日: 1997-12-03, 最終更新日: 2024-02-14)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.95 Å)