Three-dimensional structure of phosphoribosyl pyrophosphate synthetase from E. coli at 2.71 Å resolution


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Phosphoribosyl pyrophosphate synthetase from Escherichia coli was cloned, purified, and crystallized. Single crystals of the enzyme were grown under microgravity. The X-ray diffraction data set was collected at the Spring-8 synchrotron facility and used to determine the three-dimensional structure of the enzyme by the molecular-replacement method at 2.71 Å resolution. The active and regulatory sites in the molecule of E. coli phosphoribosyl pyrophosphate synthetase were revealed by comparison with the homologous protein from Bacillus subtilis, the structure of which was determined in a complex with functional ligands. The conformations of polypeptide-chain fragments surrounding and composing the active and regulatory sites were shown to be identical in both proteins.

Sobre autores

V. Timofeev

Shubnikov Institute of Crystallography; National Research Centre “Kurchatov Institute,”

Autor responsável pela correspondência
Email: inna@ns.crys.ras.ru
Rússia, Leninskii pr. 59, Moscow, 119333; pl. Akademika Kurchatova 1, Moscow, 123098

Yu. Abramchik

Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry

Email: inna@ns.crys.ras.ru
Rússia, ul. Miklukho-Maklaya 16/10, Moscow, 117997

N. Zhukhlistova

Shubnikov Institute of Crystallography

Email: inna@ns.crys.ras.ru
Rússia, Leninskii pr. 59, Moscow, 119333

T. Muravieva

Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry

Email: inna@ns.crys.ras.ru
Rússia, ul. Miklukho-Maklaya 16/10, Moscow, 117997

R. Esipov

Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry

Email: inna@ns.crys.ras.ru
Rússia, ul. Miklukho-Maklaya 16/10, Moscow, 117997

I. Kuranova

Shubnikov Institute of Crystallography; National Research Centre “Kurchatov Institute,”

Email: inna@ns.crys.ras.ru
Rússia, Leninskii pr. 59, Moscow, 119333; pl. Akademika Kurchatova 1, Moscow, 123098

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