4A8D
DegP dodecamer with bound OMP
Summary for 4A8D
Entry DOI | 10.2210/pdb4a8d/pdb |
Related | 1KY9 2J1N 2J4U |
EMDB information | 1505 |
Descriptor | PERIPLASMIC SERINE ENDOPROTEASE DEGP, OUTER MEMBRANE PROTEIN C (2 entities in total) |
Functional Keywords | hydrolase-transport protein complex, chaperone, hydrolase/transport protein |
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 | 600571.35 |
Authors | Malet, H.,Krojer, T.,Sawa, J.,Schafer, E.,Saibil, H.R.,Ehrmann, M.,Clausen, T. (deposition date: 2011-11-20, release date: 2012-01-11, Last modification date: 2024-05-08) |
Primary citation | Malet, H.,Canellas, F.,Sawa, J.,Yan, J.,Thalassinos, K.,Ehrmann, M.,Clausen, T.,Saibil, H.R. Newly Folded Substrates Inside the Molecular Cage of the Htra Chaperone Degq Nat.Struct.Mol.Biol., 19:152-, 2012 Cited by PubMed Abstract: The HtrA protein family combines chaperone and protease activities and is essential for protein quality control in many organisms. Whereas the mechanisms underlying the proteolytic function of HtrA proteins are well characterized, their chaperone activity remains poorly understood. Here we describe cryo-EM structures of Escherichia coli DegQ in its 12- and 24-mer states in complex with model substrates, providing a structural model of HtrA chaperone action. Up to six lysozyme substrates bind inside the DegQ 12-mer cage and are visualized in a close-to-native state. An asymmetric reconstruction reveals the binding of a well-ordered lysozyme to four DegQ protomers. DegQ PDZ domains are located adjacent to substrate density and their presence is required for chaperone activity. The substrate-interacting regions appear conserved in 12- and 24-mer cages, suggesting a common mechanism of chaperone function. PubMed: 22245966DOI: 10.1038/NSMB.2210 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (28 Å) |
Structure validation
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