3QO6
Crystal structure analysis of the plant protease Deg1
Summary for 3QO6
| Entry DOI | 10.2210/pdb3qo6/pdb |
| Descriptor | Protease Do-like 1, chloroplastic, peptide, ... (6 entities in total) |
| Functional Keywords | protease, htra, ph-sensor, hydrolase, photosynthesis |
| Biological source | Arabidopsis thaliana (Thale-cress) More |
| Cellular location | Plastid, chloroplast thylakoid membrane; Peripheral membrane protein; Lumenal side: O22609 |
| Total number of polymer chains | 9 |
| Total formula weight | 112762.44 |
| Authors | Clausen, T. (deposition date: 2011-02-09, release date: 2011-05-04, Last modification date: 2024-11-06) |
| Primary citation | Kley, J.,Schmidt, B.,Boyanov, B.,Stolt-Bergner, P.C.,Kirk, R.,Ehrmann, M.,Knopf, R.R.,Naveh, L.,Adam, Z.,Clausen, T. Structural adaptation of the plant protease Deg1 to repair photosystem II during light exposure. Nat.Struct.Mol.Biol., 18:728-731, 2011 Cited by PubMed Abstract: Deg1 is a chloroplastic protease involved in maintaining the photosynthetic machinery. Structural and biochemical analyses reveal that the inactive Deg1 monomer is transformed into the proteolytically active hexamer at acidic pH. The change in pH is sensed by His244, which upon protonation, repositions a specific helix to trigger oligomerization. This system ensures selective activation of Deg1 during daylight, when acidification of the thylakoid lumen occurs and photosynthetic proteins are damaged. PubMed: 21532594DOI: 10.1038/nsmb.2055 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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