PDBe 4a8b

Electron Microscopy
13Å resolution

Symmetrized cryo-EM reconstruction of E. coli DegQ 12-mer in complex with lysozymes

Released:
Related structures: EMD-1982

Function and Biology Details

Reactions catalysed:
Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl- D-glucosamine residues in chitodextrins. 
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:

Structure analysis Details

Assembly composition:
hetero 18-mer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Lysozyme C Chains: M, N, O, P, Q, R
Molecule details ›
Chains: M, N, O, P, Q, R
Length: 129 amino acids
Theoretical weight: 14.33 KDa
Source organism: Gallus gallus
UniProt:
  • Canonical: P00698 (Residues: 19-147; Coverage: 100%)
Gene name: LYZ
Sequence domains: C-type lysozyme/alpha-lactalbumin family
Periplasmic pH-dependent serine endoprotease DegQ Chains: A, B, C, D, E, F, G, H, I, J, K, L
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L
Length: 436 amino acids
Theoretical weight: 45.54 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli BL21(DE3)
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: 13Å
Relevant EMDB volumes: EMD-1982
Expression system: Escherichia coli BL21(DE3)