Brief Communication abstract
Nature Structural & Molecular Biology 16, 1192 - 1194 (2009)
Published online: 1 November 2009 | doi:10.1038/nsmb.1681
Regulation of a muralytic enzyme by dynamic membrane topology
Qingan Sun1, Gabriel F Kuty1, Arulandu Arockiasamy2, Min Xu3, Ry Young1 & James C Sacchettini1
R21, 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.
- Department of Biochemistry and Biophysics, Texas A&M University, College Station, Texas, USA.
- International Centre for Genetic Engineering and Biotechnology, Aruna Asaf Ali Marg, New Delhi, India.
- Department of Microbiology, Immunology, & Molecular Genetics, David Geffen School of Medicine at UCLA, Los Angeles, California, USA.
Correspondence to: James C Sacchettini1 e-mail: sacchett@tamu.edu
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Regulation of a muralytic enzyme by dynamic membrane topologyNature Structural & Molecular Biology Brief Communication (01 Nov 2009)
