2ZLE
Cryo-EM structure of DegP12/OMP
Summary for 2ZLE
| Entry DOI | 10.2210/pdb2zle/pdb |
| EMDB information | 1505 |
| Descriptor | Protease do, Outer membrane protein C (2 entities in total) |
| Functional Keywords | degp, htra, protease, chaperone, pdz, outer membrane protein, omp, periplasm, hydrolase, serine protease, stress response, ion transport, phage recognition, porin, transmembrane, transport |
| Biological source | Escherichia coli More |
| Cellular location | Cell inner membrane ; Peripheral membrane protein ; Cytoplasmic side : P0C0V0 Cell outer membrane; Multi-pass membrane protein: P06996 |
| Total number of polymer chains | 13 |
| Total formula weight | 600763.35 |
| Authors | Schaefer, E.,Saibil, H.R. (deposition date: 2008-04-09, release date: 2008-06-03, Last modification date: 2024-03-13) |
| Primary citation | Krojer, T.,Sawa, J.,Saibil, H.R.,Ehrmann, M.,Clausen, T. Structural basis for the regulated protease and chaperone function of DegP Nature, 453:885-890, 2008 Cited by PubMed Abstract: All organisms have to monitor the folding state of cellular proteins precisely. The heat-shock protein DegP is a protein quality control factor in the bacterial envelope that is involved in eliminating misfolded proteins and in the biogenesis of outer-membrane proteins. Here we describe the molecular mechanisms underlying the regulated protease and chaperone function of DegP from Escherichia coli. We show that binding of misfolded proteins transforms hexameric DegP into large, catalytically active 12-meric and 24-meric multimers. A structural analysis of these particles revealed that DegP represents a protein packaging device whose central compartment is adaptable to the size and concentration of substrate. Moreover, the inner cavity serves antagonistic functions. Whereas the encapsulation of folded protomers of outer-membrane proteins is protective and might allow safe transit through the periplasm, misfolded proteins are eliminated in the molecular reaction chamber. Oligomer reassembly and concomitant activation on substrate binding may also be critical in regulating other HtrA proteases implicated in protein-folding diseases. PubMed: 18496527DOI: 10.1038/nature07004 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (28 Å) |
Structure validation
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