6if4

Publication Abstract from PubMed

The essential SAS2-related acetyltransferase 1 (Esa1), as a acetyltransferase of MYST family, is indispensable for the cell cycle and transcriptional regulation. The Tudor domain consists of 60 amino acids and belongs to the Royal family, which serves as a module interacting with methylated histone and/or DNA. Although Tudor domain has been widely studied in higher eukaryotes, its structure and function remain unclear in Trypanosoma brucei (T. brucei), a protozoan unicellular parasite causing sleeping sickness in human and nagana in cattle in sub-Saharan Africa. Here, we determined a high-resolution structure of TbEsa1 presumed Tudor domain from T. brucei by X-ray crystallography. TbEsa1 Tudor domain adopts a conserved Tudor-like fold, which is comprised of a five-stranded beta-barrel surrounded by two short alpha-helices. Furthermore, we revealed a non-specific DNA binding pattern of TbEsa1 Tudor domain. However, TbEsa1 Tudor domain showed no methyl-histone binding ability, due to the absence of key aromatic residues forming a conserved aromatic cage.

Crystal structure of TbEsa1 presumed Tudor domain from Trypanosoma brucei.,Gao J, Ye K, Diwu Y, Xu C, Zhang X, Liao S, Tu X J Struct Biol. 2020 Jan 1;209(1):107406. doi: 10.1016/j.jsb.2019.107406. Epub, 2019 Nov 17. PMID:31747559^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.