1XJT

Crystal structure of active form of P1 phage endolysin Lyz

Summary for 1XJT

Entry DOI	10.2210/pdb1xjt/pdb
Related	1XJU
Descriptor	Lysozyme, CITRIC ACID (3 entities in total)
Functional Keywords	open conformation, hydrolase
Biological source	Enterobacteria phage P1
Total number of polymer chains	1
Total formula weight	21871.60
Authors	Arockiasamy, A.,Sacchettini, J.C. (deposition date: 2004-09-24, release date: 2005-01-11, Last modification date: 2024-10-09)
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 Cited by 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 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.75 Å)

Structure validation