X‐Ray crystallographic studies of recombinant inorganic pyrophosphatase from Escherichia coli

FEBS Letters

Popov, A.N.¹  Vorobyeva, N.N.³  Nazarova, T.I.²  Harutyunyan, E.H.¹  Kurilova, S.A.²  Avaeva, S.M.²  Oganessyan, V.Yu.¹  Lebedev, A.A.¹ 

[1] Institute of Crystallography, Russian Academy of Sciences, Leninsky pr. 59, Moscow 117333, Russian Federation;A.N. Belozersky Institute of Physico-Chemical Biology and Moscow State University, Moscow, Russian Federation;Chemical Department, Moscow State University, Moscow, Russian Federation

关键词: E. coli inorganic pyrophosphatase;    X-ray structure;    Recombinant vector;    Expression;   

DOI  :  10.1016/0014-5793(94)00605-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

An E. coli inorganic pyrophosphatase overproducer and a method for a large-scale production of the homogeneous enzyme are described. The inorganic pyrophosphatase was crystallized in the form containing one subunit of a homohexameric molecule per asymmetric unit: space group R32, a = 110.4 Å, c = 76.8 Å. The electron density map to 2.5 Å resolution phased with Eu- and Hg-derivatives (figure of merit, <m> = 0.51) was improved by the solvent flattening procedure (<m> = 0.77). The course of the polypeptide chain and the secondary structure elements, intersubunit contacts and positions of the active sites were characterized. Homology with S. cerevisiae inorganic pyrophosphatase structure was found.

【 授权许可】

Unknown