Crystallization in Microgravity and the Atomic-Resolution Structure of Uridine Phosphorylase from Vibrio cholerae

P. A. Eistrikh-Heller, S. V. Rubinsky, V. R. Samygina, A. G. Gabdulkhakov, M. V. Kovalchuk, A. S. Mironov, A. A. Lashkov

Research output: Contribution to journalArticlepeer-review

Abstract

Abstract: Uridine phosphorylases are known as key targets for the development of new anticancer and antiparasitic agents. Crystals of uridine phosphorylase from the pathogenic bacterium Vibrio cholerae were grown in microgravity by the capillary counter-diffusion method on board of the International Space Station. The three-dimensional structure of this enzyme was determined at atomic (1.04 Å) resolution (RCSB PDB ID: 6Z9Z). Alternative conformations of long fragments (β-strands and adjacent loops) of the protein molecule were found for the first time in the three-dimensional structure of uridine phosphorylase in the absence of specific bound ligands. Apparently, these alternative conformations are related to the enzyme function. Conformational analysis with Markov state models demonstrated that conformational rearrangements can occur in the ligand-free state of the enzyme.

Original languageEnglish
Pages (from-to)777-785
Number of pages9
JournalCrystallography Reports
Volume66
Issue number5
DOIs
StatePublished - Sep 2021
Externally publishedYes

Scopus subject areas

  • Condensed Matter Physics
  • Chemistry(all)
  • Materials Science(all)

Keywords

  • PRELIMINARY-X-RAY
  • MOLECULAR-DYNAMICS
  • COMPLEX
  • EXPRESSION
  • MECHANISM
  • PROTEIN

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