title: Regulation of a muralytic enzyme by dynamic membrane topology.
abstract: 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.
authors.affiliation: Department of Biochemistry and Biophysics, Texas A&M University, College Station, Texas, USA.
authors.forename: Qingan
authors.initials: Q
authors.lastname: Sun
authors.forename: Gabriel F
authors.initials: GF
authors.lastname: Kuty
authors.forename: Arulandu
authors.initials: A
authors.lastname: Arockiasamy
authors.forename: Min
authors.initials: M
authors.lastname: Xu
authors.forename: Ry
authors.initials: R
authors.lastname: Young
authors.forename: James C
authors.initials: JC
authors.lastname: Sacchettini
mesh_terms: 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*
chemical_list: D014764:Viral Proteins; D009113:Muramidase