6KUI
Active conformation of HslV from Staphylococcus aureus.
Summary for 6KUI
| Entry DOI | 10.2210/pdb6kui/pdb |
| Related | 6KR1 |
| Descriptor | ATP-dependent protease subunit HslV (2 entities in total) |
| Functional Keywords | hslv, bacterial proteasome, threonine protease, protease, hydrolase |
| Biological source | Staphylococcus aureus (strain Mu50 / ATCC 700699) |
| Total number of polymer chains | 3 |
| Total formula weight | 64909.70 |
| Authors | |
| 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 Cited by 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: 32694241DOI: 10.14348/molcells.2020.0074 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.33 Å) |
Structure validation
Download full validation report
