› 4a9g

Electron Microscopy
7.5Å resolution

Symmetrized cryo-EM reconstruction of E. coli DegQ 24-mer in complex with beta-casein

Released:
DOI: 10.2210/pdb4a9g/pdb
PDB entry 4a9g coloured by chain, front view.
PDB entry 4a9g coloured by chain, side view.
PDB entry 4a9g coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Newly folded substrates inside the molecular cage of the HtrA chaperone DegQ.
Malet H, Canellas F, Sawa J, Yan J, Thalassinos K, Ehrmann M, Clausen T, Saibil HR
Nat Struct Mol Biol 19 152-7 (2012)
PMID: 22245966
Related structures: EMD-1984

Function and Biology Details

Reaction catalysed: 
Acts on substrates that are at least partially unfolded. The cleavage site P1 residue is normally between a pair of hydrophobic residues, such as Val-|-Val
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo 24-mer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153828 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Periplasmic pH-dependent serine endoprotease DegQ Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, Y
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, Y
Length: 436 amino acids
Theoretical weight: 45.54 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P39099 (Residues: 28-455; Coverage: 100%)
Gene names: JW3203, b3234, degQ, hhoA
Sequence domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 7.5Å
Relevant EMDB volumes: EMD-1984
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Autotransporter secretion: varying on a theme.
Grijpstra et al. (2013)
5 more

3 mentions without citation

Newly folded substrates inside the molecular cage of the HtrA chaperone DegQ.
Malet et al. (2012)
2 more