Cleavage-Dependent Activation of ATP-Dependent Protease HslUV from Staphylococcus aureus.

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 Staphylococcus aureus 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 A

SUBMITTER: Jeong S 

PROVIDER: S-EPMC7468587 | biostudies-literature | 2020 Aug

REPOSITORIES: biostudies-literature