1XJU: Crystal Structure Of Secreted Inactive Form Of P1 Phage Endolysin Lyz

The P1 lysozyme Lyz is secreted to the periplasm of Escherichia coli and accumulates in an inactive membrane-tethered form. Genetic and biochemical experiments show that, when released from the bilayer, Lyz is activated by an intramolecular thiol-disulfide isomerization, which requires a cysteine in its N-terminal SAR (signal-arrest-release) domain. Crystal structures confirm the alternative disulfide linkages in the two forms of Lyz and reveal dramatic conformational differences in the catalytic domain. Thus, the exported P1 endolysin is kept inactive by three levels of control-topological, conformational, and covalent-until its release from the membrane is triggered by the P1 holin.
PDB ID: 1XJUDownload
MMDB ID: 31441
PDB Deposition Date: 2004/9/24
Updated in MMDB: 2017/11
Experimental Method:
x-ray diffraction
Resolution: 1.07  Å
Source Organism:
Similar Structures:
Biological Unit for 1XJU: monomeric; determined by author and by software (PQS)
Molecular Components in 1XJU
Label Count Molecule
Protein (1 molecule)
Lysozyme(Gene symbol: lyz)
Molecule annotation
Chemicals (2 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB