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

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.
Authors:
 [1] ;  [2] ;  [1] ; ;  [2] ;  [1]
  1. Russian Academy of Sciences, Shubnikov Institute of Crystallography (Russian Federation)
  2. Russian Academy of Sciences, Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry (Russian Federation)
Publication Date:
OSTI Identifier:
22471925
Resource Type:
Journal Article
Resource Relation:
Journal Name: Crystallography Reports; Journal Volume: 61; Journal Issue: 1; Other Information: Copyright (c) 2016 Pleiades Publishing, Inc.; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United States
Language:
English
Subject:
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; BACILLUS SUBTILIS; COMPARATIVE EVALUATIONS; ESCHERICHIA COLI; LIGANDS; LIGASES; MOLECULES; MONOCRYSTALS; POLYPEPTIDES; PROTEIN STRUCTURE; SPRING-8 STORAGE RING; THREE-DIMENSIONAL LATTICES; X-RAY DIFFRACTION