Crystal structure of Escherichia coli inorganic pyrophosphatase complexed with SO4 2−

FEBS Letters

Dauter, Zbygnew³  Sklyankina, Vera¹  Huber, Robert⁵  Oganessyan, Vaheh²  Kurilova, Svetlana⁴  Vorobyeva, Natalya¹  Rodina, Elena⁴  Harutyunyan, Emil²  Mather, Timothy⁵  Nazarova, Tatjana⁴  Grigorjeva, Olga¹  Avaeva, Svetlana⁴  Wilson, Keith³ 

[1] Chemistry Department, Moscow State University, Moscow, Russia;Institute of Crystallography, Russian Academy of Sciences, Moscow, Russia;EMBL Outstation c/o DESY, Hamburg, Germany;A.N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, Vorobyevy Gory, MSU, Moscow 119899, Russia;Institute of Biochemistry, Munich, Germany

关键词: Inorganic pyrophosphatase;    Escherichia coli;    Crystal structure;    Complex with sulfate;    Cooperativity;   

DOI  :  10.1016/S0014-5793(97)00650-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The three-dimensional structure of inorganic pyrophosphatase from Escherichia coli complexed with sulfate was determined at 2.2 Å resolution using Patterson's search technique and refined to an R-factor of 19.2%. Sulfate may be regarded as a structural analog of phosphate, the product of the enzyme reaction, and as a structural analog of methyl phosphate, the irreversible inhibitor. Sulfate binds to the pyrophosphatase active site cavity as does phosphate and this diminishes molecular symmetry, converting the homohexamer structure form (α₃)₂ into α₃′α₃″. The asymmetry of the molecule is manifested in displacements of protein functional groups and some parts of the polypeptide chain and reflects the interaction of subunits and their cooperation. The significance of re-arrangements for pyrophosphatase function is discussed.

【 授权许可】

Unknown