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TitleNewly folded substrates inside the molecular cage of the HtrA chaperone DegQ.
Journal, issue, pagesNat Struct Mol Biol, Vol. 19, Issue 2, Page 152-157, Year 2012
Publish dateJan 15, 2012
AuthorsHélène Malet / Flavia Canellas / Justyna Sawa / Jun Yan / Konstantinos Thalassinos / Michael Ehrmann / Tim Clausen / Helen R Saibil /
PubMed AbstractThe 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 ...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.
External linksNat Struct Mol Biol / PubMed:22245966 / PubMed Central
MethodsEM (single particle)
Resolution7.5 - 28 Å
Structure data

1981

4a8a

EMDB-1981, PDB-4a8a:
Asymmetric cryo-EM reconstruction of E. coli DegQ 12-mer in complex with lysozyme
Method: EM (single particle) / Resolution: 14.2 Å

1982

4a8b

EMDB-1982, PDB-4a8b:
Symmetrized cryo-EM reconstruction of E. coli DegQ 12-mer in complex with lysozymes
Method: EM (single particle) / Resolution: 13.0 Å

1983

4a8c

EMDB-1983, PDB-4a8c:
Symmetrized cryo-EM reconstruction of E. coli DegQ 12-mer in complex with a binding peptide
Method: EM (single particle) / Resolution: 7.5 Å

1984

4a9g

EMDB-1984, PDB-4a9g:
Symmetrized cryo-EM reconstruction of E. coli DegQ 24-mer in complex with beta-casein
Method: EM (single particle) / Resolution: 7.5 Å

PDB-4a8d:
DegP dodecamer with bound OMP
Method: ELECTRON MICROSCOPY / Resolution: 28.0 Å

Source
  • escherichia coli (E. coli)
  • gallus gallus (chicken)
  • synthetic construct (others)
  • Bos taurus (cattle)
KeywordsHYDROLASE/HYDROLASE / HYDROLASE-HYDROLASE COMPLEX / CHAPERONE / HYDROLASE / HYDROLASE/TRANSPORT PROTEIN / HYDROLASE-TRANSPORT PROTEIN COMPLEX

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