6V6H

Crystal structure of histidine ammonia-lyase from Trypanosoma cruzi

Summary for 6V6H

• Entry DOI: 10.2210/pdb6v6h/pdb
• Descriptor: Histidine ammonia-lyase (2 entities in total)
• Functional Keywords: histidine ammonia-lyase, protection domain absence, lyase
• Biological source: Trypanosoma cruzi
• Total number of polymer chains: 4
• Total formula weight: 235979.62

Authors

Miranda, R.R.,Silva, M.,Barison, M.J.,Silber, A.M.,Iulek, J. (deposition date: 2019-12-05, release date: 2020-06-10, Last modification date: 2024-11-13)

Primary citation

Miranda, R.R.,Silva, M.,Barison, M.J.,Silber, A.M.,Iulek, J.
Crystal structure of histidine ammonia-lyase from Trypanosoma cruzi.
Biochimie, 175:181-188, 2020

PubMed Abstract: Chagas 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 2.55 Å 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.

PubMed: 32464165
DOI: 10.1016/j.biochi.2020.05.009

Experimental method

X-RAY DIFFRACTION (2.55 Å)