1XJU

Crystal structure of secreted inactive form of P1 phage endolysin Lyz

Summary for 1XJU

• Entry DOI: 10.2210/pdb1xju/pdb
• Descriptor: Lysozyme, SULFATE ION (3 entities in total)
• Functional Keywords: secreted inactive conformation, hydrolase
• Biological source: Enterobacteria phage P1
• Total number of polymer chains: 2
• Total formula weight: 37726.44

Authors

Arockiasamy, A.,Sacchettini, J.C. (deposition date: 2004-09-24, release date: 2005-01-11, Last modification date: 2024-10-30)

Primary citation

Xu, M.,Arulandu, A.,Struck, D.K.,Swanson, S.,Sacchettini, J.C.,Young, R.
Disulfide isomerization after membrane release of its SAR domain activates P1 lysozyme.
Science, 307:113-117, 2005

PubMed Abstract: 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.

PubMed: 15637279
DOI: 10.1126/science.1105143

Experimental method

X-RAY DIFFRACTION (1.07 Å)