Regulation of a muralytic enzyme by dynamic membrane topology.
R(21), the lysozyme of coliphage 21, has an N-terminal signal-anchor-release (SAR) domain that directs its secretion in a membrane-tethered, inactive form and then its release and activation in the periplasm. Both genetic and crystallographic studies show that the SAR domain, once extracted from the bilayer, refolds into the body of the enzyme and effects muralytic activation by repositioning one residue of the canonical lysozyme catalytic triad.
Sun
Qingan
Q
Department of Biochemistry and Biophysics, Texas A&M University, College Station, Texas, USA.
Kuty
Gabriel F
GF
Arockiasamy
Arulandu
A
Xu
Min
M
Young
Ry
R
Sacchettini
James C
JC
D017101:Bacteriophage P1 / Q000378:metabolism*; D003090:Coliphages / Q000378:metabolism*; D009113:Muramidase / Q000737:chemistry* / Q000378:metabolism*; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D014764:Viral Proteins / Q000737:chemistry* / Q000378:metabolism*
D014764:Viral Proteins; D009113:Muramidase