6IF4

Crystal structure of Tbtudor

Summary for 6IF4

• Entry DOI: 10.2210/pdb6if4/pdb
• Descriptor: Histone acetyltransferase (2 entities in total)
• Functional Keywords: tudor, dna, transcription, methylation, dna binding protein
• Biological source: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
• Total number of polymer chains: 2
• Total formula weight: 17139.30

Authors

Gao, J.,Ye, K.,Diwu, Y.,Liao, S.,Tu, X. (deposition date: 2018-09-18, release date: 2019-09-18, Last modification date: 2023-11-22)

Primary citation

Gao, J.,Ye, K.,Diwu, Y.,Xu, C.,Zhang, X.,Liao, S.,Tu, X.
Crystal structure of TbEsa1 presumed Tudor domain from Trypanosoma brucei.
J.Struct.Biol., 209:107406-107406, 2020

PubMed Abstract: 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 β-barrel surrounded by two short α-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.

PubMed: 31747559
DOI: 10.1016/j.jsb.2019.107406

Experimental method

X-RAY DIFFRACTION (1.934 Å)