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.
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References
McPherson A, Cudney B (2014) Optimization of crystallization conditions for biological macromolecules. Acta Crystallogr F Struct Biol Commun 70:1445–1467
McPherson A, Malkin AJ, Kuznetsov YG (1995) The science of macromolecular crystallization. Structure 3:759–768
Chayen NE (2009) High-throughput protein crystallization. Adv Protein Chem Struct Biol 77:1–22
Trasvina-Arenas CH, Lopez-Castillo LM, Sanchez-Sandoval E, Brieba LG (2016) Dispensability of the [4Fe-4S] cluster in novel homologues of adenine glycosylase MutY. FEBS J 283:521–540
Castro-Torres E, Jimenez-Sandoval P, Fernandez-de Gortari E, Lopez-Castillo M, Baruch-Torres N, Lopez-Hidalgo M, Peralta-Castro A, Diaz-Quezada C, Sotelo-Mundo RR, Benitez-Cardoza CG, Espinoza-Fonseca LM, Ochoa-Leyva A, Brieba LG (2018) Structural basis for the limited response to oxidative and Thiol-conjugating agents by triosephosphate Isomerase from the photosynthetic bacteria synechocystis. Front Mol Biosci 5:103
Castro-Torres E, Jimenez-Sandoval P, Romero-Romero S, Fuentes-Pascacio A, Lopez-Castillo LM, Diaz-Quezada C, Fernandez-Velasco DA, Torres-Larios A, Brieba LG (2019) Structural basis for the modulation of plant cytosolic triosephosphate isomerase activity by mimicry of redox-based modifications. Plant J 99(5):950–964
Lopez-Zavala AA, Carrasco-Miranda JS, Ramirez-Aguirre CD, Lopez-Hidalgo M, Benitez-Cardoza CG, Ochoa-Leyva A, Cardona-Felix CS, Diaz-Quezada C, Rudino-Pinera E, Sotelo-Mundo RR, Brieba LG (2016) Structural insights from a novel invertebrate triosephosphate isomerase from Litopenaeus vannamei. Biochim Biophys Acta 1864:1696–1706
Zhu K, Jin H, He Z, Zhu Q, Wang B (2006) A continuous method for the large-scale extraction of plasmid DNA by modified boiling lysis. Nat Protoc 1:3088–3093
Acknowledgments
We thank “Programa de Salud de la Fundación Miguel Alemán A. C (México)” for funding. We thank Daniela Camacho and Lucia Leyva for their help during crystallogenesis and Misraim Gurrola for his interest in epidemiology that initiated this study.
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Jimenez-Sandoval, P., Castro-Torres, E., Diaz-Quezada, C., Brieba, L.G. (2020). Crystallographic Studies of Triosephosphate Isomerase from Schistosoma mansoni. In: Timson, D.J. (eds) Schistosoma mansoni. Methods in Molecular Biology, vol 2151. Humana, New York, NY. https://doi.org/10.1007/978-1-0716-0635-3_17
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DOI: https://doi.org/10.1007/978-1-0716-0635-3_17
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Publisher Name: Humana, New York, NY
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Online ISBN: 978-1-0716-0635-3
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