Solution structure of a ubiquitin-like protein from Trypanosoma brucei
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چکیده
منابع مشابه
Crystal structure of a Trypanosoma brucei metacaspase.
Metacaspases are distantly related caspase-family cysteine peptidases implicated in programmed cell death in plants and lower eukaryotes. They differ significantly from caspases because they are calcium-activated, arginine-specific peptidases that do not require processing or dimerization for activity. To elucidate the basis of these differences and to determine the impact they might have on th...
متن کاملProtein isoprenylation in Trypanosoma brucei brucei.
Trypanosoma brucei is a digenetic protozoan parasite presenting a public health hazard in certain areas of Africa; it is transmitted between mammals (bloodstream form (BSF)) by tsetse flies (procyclic form (PCF)). We have an ongoing interest in small GTP proteins in T. brucei, and these are commonly isoprenylated. Many isoprenylated proteins belong to the rab family and include ras; the isopren...
متن کاملCrystal Structure of an Arginase-like Protein from Trypanosoma brucei That Evolved without a Binuclear Manganese Cluster
The X-ray crystal structure of an arginase-like protein from the parasitic protozoan Trypanosoma brucei, designated TbARG, is reported at 1.80 and 2.38 Å resolution in its reduced and oxidized forms, respectively. The oxidized form of TbARG is a disulfide-linked hexamer that retains the overall architecture of a dimer of trimers in the reduced form. Intriguingly, TbARG does not contain metal io...
متن کاملA Protein Complex Map of Trypanosoma brucei
The functions of the majority of trypanosomatid-specific proteins are unknown, hindering our understanding of the biology and pathogenesis of Trypanosomatida. While protein-protein interactions are highly informative about protein function, a global map of protein interactions and complexes is still lacking for these important human parasites. Here, benefiting from in-depth biochemical fraction...
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ژورنال
عنوان ژورنال: Protein Science
سال: 2018
ISSN: 0961-8368
DOI: 10.1002/pro.3492