Crystallographic Studies of Triosephosphate Isomerase from Schistosoma mansoni

Methods Mol Biol. 2020:2151:211-218. doi: 10.1007/978-1-0716-0635-3_17.

Abstract

Protein structure determination by X-ray crystallography guides structure-function and rational drug design studies. Helminths cause devastating diseases, including schistosomiasis that affects over one-third of the human population. Trematodes from the genus Schistosoma heavily depend on glycolysis; thus enzymes involved in this metabolic pathway are potential drug targets. Here we present a protocol to obtain crystal structures of recombinantly expressed triosephosphate isomerase from S. mansoni (SmTPI) that diffracted in house to a resolution of 2 Å.

Keywords: Protein crystallography; Recombinant expression; Synthetic gene; Triosephosphate isomerase.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Crystallization
  • Crystallography, X-Ray / methods*
  • Gene Expression
  • Genetic Vectors / metabolism
  • Schistosoma mansoni / enzymology*
  • Triose-Phosphate Isomerase / chemistry*
  • Triose-Phosphate Isomerase / genetics
  • Triose-Phosphate Isomerase / isolation & purification

Substances

  • Triose-Phosphate Isomerase