6TV6
Octameric McsB from Bacillus subtilis.
Summary for 6TV6
| Entry DOI | 10.2210/pdb6tv6/pdb |
| Descriptor | Protein-arginine kinase, MAGNESIUM ION (3 entities in total) |
| Functional Keywords | phosho-arginine-kinase, transferase |
| Biological source | Bacillus subtilis (strain 168) |
| Total number of polymer chains | 4 |
| Total formula weight | 170534.53 |
| Authors | Suskiewicz, M.J.,Hajdusits, B.,Meinhart, A.,Clausen, T. (deposition date: 2020-01-09, release date: 2021-07-21, Last modification date: 2024-01-24) |
| Primary citation | Hajdusits, B.,Suskiewicz, M.J.,Hundt, N.,Meinhart, A.,Kurzbauer, R.,Leodolter, J.,Kukura, P.,Clausen, T. McsB forms a gated kinase chamber to mark aberrant bacterial proteins for degradation. Elife, 10:-, 2021 Cited by PubMed Abstract: In Gram-positive bacteria, the McsB protein arginine kinase is central to protein quality control, labeling aberrant molecules for degradation by the ClpCP protease. Despite its importance for stress response and pathogenicity, it is still elusive how the bacterial degradation labeling is regulated. Here, we delineate the mechanism how McsB targets aberrant proteins during stress conditions. Structural data reveal a self-compartmentalized kinase, in which the active sites are sequestered in a molecular cage. The 'closed' octamer interconverts with other oligomers in a phosphorylation-dependent manner and, unlike these 'open' forms, preferentially labels unfolded proteins. In vivo data show that heat-shock triggers accumulation of higher order oligomers, of which the octameric McsB is essential for surviving stress situations. The interconversion of open and closed oligomers represents a distinct regulatory mechanism of a degradation labeler, allowing the McsB kinase to adapt its potentially dangerous enzyme function to the needs of the bacterial cell. PubMed: 34328418DOI: 10.7554/eLife.63505 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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