期刊
JOURNAL OF STRUCTURAL BIOLOGY
卷 209, 期 1, 页码 -出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.jsb.2019.107406
关键词
TbEsa1; Tudor domain; X-ray crystallography; NMR; DNA binding; T. brucei
资金
- Fundamental Research Funds for the Central Universities [WK9110000042]
- Major/Innovative Program of the Development Foundation of the Hefei Center for Physical Science and Technology [2018CXFX007]
- Chinese National Natural Science Foundation [U1332137, 31500601, 31570737]
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.
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