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Small-Angle X-ray Scattering Study of Changes in the Quaternary Structure of Nucleotide-Regulated Pyrophosphatase from Desulfitobacterium hafniense upon Ligand Binding in Solution

Authors
  • Dadinova, L. A.1
  • Anashkin, V. A.2
  • Shtykova, E. V.1
  • 1 Shubnikov Institute of Crystallography of Federal Scientific Research Centre “Crystallography and Photonics”, Russian Academy of Sciences, Moscow, 119333, Russia , Moscow (Russia)
  • 2 Belozersky Institute of Physico-Chemical Biology, Moscow State University, Moscow, 119992, Russia , Moscow (Russia)
Type
Published Article
Journal
Crystallography Reports
Publisher
Pleiades Publishing
Publication Date
Sep 01, 2020
Volume
65
Issue
5
Pages
749–754
Identifiers
DOI: 10.1134/S1063774520050053
Source
Springer Nature
License
Yellow

Abstract

AbstractThe regulation of nucleotide-regulated inorganic pyrophosphatases at a molecular level has been extensively studied in order to establish the mechanism of signal transduction between the active and regulatory sites of these enzymes. However, this issue cannot be ultimately addressed because of the lack of reliable structural data on the full-length protein and its interactions with ligands. The low-resolution structure of nucleotide-regulated pyrophosphatase from Desulfitobacterium hafniense was determined for the first time by small-angle X-ray scattering. The structural changes in the full-length enzyme upon binding of adenosine monophosphate and diadenosine tetraphosphate were revealed. In dilute solutions the protein was found to exist as a stable homotetramer, the structure of which depends on the nature of the bound ligand. The structural data are important for an understanding of the molecular basis for regulation of this family of enzymes.

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