7FER
Cryo-EM structure of BsClpP-ADEP1 complex at pH 4.2
Summary for 7FER
| Entry DOI | 10.2210/pdb7fer/pdb |
| EMDB information | 31561 |
| Related PRD ID | PRD_000503 |
| Descriptor | ATP-dependent Clp protease proteolytic subunit, ADEP1 (2 entities in total) |
| Functional Keywords | clpp, bacillus subtilis, hydrolase, adep1 |
| Biological source | Bacillus subtilis More |
| Total number of polymer chains | 28 |
| Total formula weight | 323981.27 |
| Authors | Kim, L.,Lee, B.-G.,Kim, M.K.,Kwon, D.H.,Kim, H.,Brotz-Oesterhelt, H.,Roh, S.-H.,Song, H.K. (deposition date: 2021-07-21, release date: 2022-07-06, Last modification date: 2022-07-20) |
| Primary citation | Kim, L.,Lee, B.G.,Kim, M.,Kim, M.K.,Kwon, D.H.,Kim, H.,Brotz-Oesterhelt, H.,Roh, S.H.,Song, H.K. Structural insights into ClpP protease side exit pore-opening by a pH drop coupled with substrate hydrolysis. Embo J., 41:e109755-e109755, 2022 Cited by PubMed Abstract: The ClpP serine peptidase is a tetradecameric degradation molecular machine involved in many physiological processes. It becomes a competent ATP-dependent protease when coupled with Clp-ATPases. Small chemical compounds, acyldepsipeptides (ADEPs), are known to cause the dysregulation and activation of ClpP without ATPases and have potential as novel antibiotics. Previously, structural studies of ClpP from various species revealed its structural details, conformational changes, and activation mechanism. Although product release through side exit pores has been proposed, the detailed driving force for product release remains elusive. Herein, we report crystal structures of ClpP from Bacillus subtilis (BsClpP) in unforeseen ADEP-bound states. Cryo-electron microscopy structures of BsClpP revealed various conformational states under different pH conditions. To understand the conformational change required for product release, we investigated the relationship between substrate hydrolysis and the pH-lowering process. The production of hydrolyzed peptides from acidic and basic substrates by proteinase K and BsClpP lowered the pH values. Our data, together with those of previous findings, provide insight into the molecular mechanism of product release by the ClpP self-compartmentalizing protease. PubMed: 35593068DOI: 10.15252/embj.2021109755 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.4 Å) |
Structure validation
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