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Crystal structure of histidine ammonia-lyase from Trypanosoma cruziCrystal structure of histidine ammonia-lyase from Trypanosoma cruzi
Structural highlights
FunctionPublication Abstract from PubMedChagas disease is one of seventeen neglected tropical diseases according to the World Health Organization (WHO). The histidine-glutamate metabolic pathway is an oxidative route that has shown to be relevant for the bioenergetics in Trypanosoma cruzi, the etiological agent for Chagas disease. Histidine ammonia-lyase participates in the first stage of the histidine catabolism, catalyzing the conversion of l-histidine into urocanate. This work presents the three-dimensional (3D) structure of Trypanosoma cruzi histidine ammonia-lyase enzyme (TcHAL) and some comparisons of it to homologous structures. The enzyme was expressed, purified and assayed for crystallization, what allowed the obtainment of crystals of sufficient quality to collect X-ray diffraction data up to 2.55A resolution. After refinement, some structural analyses indicated that the structure does not contain the active site protection domain, in opposition to previously known 3D structures from plants and fungi phenylalanine ammonia-lyase, therefore, it is the first structure of eukaryotic ammonia-lyases that lacks this domain. Crystal structure of histidine ammonia-lyase from Trypanosoma cruzi.,Miranda RR, Silva M, Barison MJ, Silber AM, Iulek J Biochimie. 2020 May 25. pii: S0300-9084(20)30118-8. doi:, 10.1016/j.biochi.2020.05.009. PMID:32464165[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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