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4HO7

Crystal structure of eukaryotic HslV from Trypanosoma brucei

Summary for 4HO7
Entry DOI10.2210/pdb4ho7/pdb
Related4HNZ
DescriptorHslVU complex proteolytic subunit, putative, MAGNESIUM ION (3 entities in total)
Functional Keywordsmitochondria, hydrolase
Biological sourceTrypanosoma brucei brucei
Total number of polymer chains3
Total formula weight58765.36
Authors
Sung, K.H.,Lee, S.Y.,Song, H.K. (deposition date: 2012-10-22, release date: 2013-07-10, Last modification date: 2024-02-28)
Primary citationSung, K.H.,Lee, S.Y.,Song, H.K.
Structural and Biochemical Analyses of the Eukaryotic Heat Shock Locus V (HslV) from Trypanosoma brucei.
J.Biol.Chem., 288:23234-23243, 2013
Cited by
PubMed Abstract: In many bacteria, heat shock locus V (HslV) functions as a protease, which is activated by heat shock locus U (HslU). The primary sequence and structure of HslV are well conserved with those of the β-subunit of the 20 S proteasome core particle in eukaryotes. To date, the HslVU complex has only been characterized in the prokaryotic system. Recently, however, the coexistence of a 20 S proteasome with HslV protease in the same living organism has been reported. In Trypanosoma brucei, a protozoan parasite that causes human sleeping sickness in Africa, HslV is localized in the mitochondria, where it has a novel function in regulating mitochondrial DNA replication. Although the prokaryotic HslVU system has been studied extensively, little is known regarding its eukaryotic counterpart. Here, we report the biochemical characteristics of an HslVU complex from T. brucei. In contrast to the prokaryotic system, T. brucei possesses two potential HslU molecules, and we found that only one of them activates HslV. A key activating residue, Tyr(494), was identified in HslU2 by biochemical and mutational studies. Furthermore, to our knowledge, this study is the first to report the crystal structure of a eukaryotic HslV, determined at 2.4 Å resolution. Drawing on our comparison of the biochemical and structural data, we discuss herein the differences and similarities between eukaryotic and prokaryotic HslVs.
PubMed: 23818520
DOI: 10.1074/jbc.M113.484832
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.601 Å)
Structure validation

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