6KWW

HslU from Staphylococcus aureus

Summary for 6KWW

• Entry DOI: 10.2210/pdb6kww/pdb
• Descriptor: ATP-dependent protease ATPase subunit HslU (1 entity in total)
• Functional Keywords: hslu, clpy, aaa+atpase, protein unfolding, chaperone
• Biological source: Staphylococcus aureus subsp. aureus Mu50
• Total number of polymer chains: 24
• Total formula weight: 1296706.13

Authors

Ha, N.-C.,Jeong, S. (deposition date: 2019-09-09, release date: 2020-07-15, Last modification date: 2023-11-22)

Primary citation

Jeong, S.,Ahn, J.,Kwon, A.R.,Ha, N.-C.
Cleavage-Dependent Activation of ATP-Dependent Protease HslUV from Staphylococcus aureus .
Mol.Cells, 43:694-704, 2020

PubMed Abstract: HslUV is a bacterial heat shock protein complex consisting of the AAA+ ATPase component HslU and the protease component HslV. HslV is a threonine (Thr) protease employing the N-terminal Thr residue in the mature protein as the catalytic residue. To date, HslUV from Gram-negative bacteria has been extensively studied. However, the mechanisms of action and activation of HslUV from Gram-positive bacteria, which have an additional N-terminal sequence before the catalytic Thr residue, remain to be revealed. In this study, we determined the crystal structures of HslV from the Gram-positive bacterium with and without HslU in the crystallization conditions. The structural comparison suggested that a structural transition to the symmetric form of HslV was triggered by ATP-bound HslU. More importantly, the additional N-terminal sequence was cleaved in the presence of HslU and ATP, exposing the Thr9 residue at the N-terminus and activating the ATP-dependent protease activity. Further biochemical studies demonstrated that the exposed N-terminal Thr residue is critical for catalysis with binding to the symmetric HslU hexamer. Since eukaryotic proteasomes have a similar additional N-terminal sequence, our results will improve our understanding of the common molecular mechanisms for the activation of proteasomes.

PubMed: 32694241
DOI: 10.14348/molcells.2020.0074

Experimental method

X-RAY DIFFRACTION (3 Å)