Regulation of a muralytic enzyme by dynamic membrane topology. Academic Article

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

• Sacchettini, James
• Young, Ryland

published proceedings

• Nat Struct Mol Biol

author list (cited authors)

• Sun, Q., Kuty, G. F., Arockiasamy, A., Xu, M., Young, R. y., & Sacchettini, J. C.

citation count

• 46

complete list of authors

• Sun, Qingan||Kuty, Gabriel F||Arockiasamy, Arulandu||Xu, Min||Young, Ry||Sacchettini, James C

publication date

• January 2009

publisher

• Springer Nature  Publisher

published in

• Nature Structural and Molecular Biology  Journal

keywords

• Bacteriophage P1
• Coliphages
• Muramidase
• Protein Structure, Secondary
• Protein Structure, Tertiary
• Viral Proteins

Digital Object Identifier (DOI)

• 10.1038/nsmb.1681

start page

• 1192

end page

• 1194

volume

• 16

issue

• 11

URL

• http://dx.doi.org/10.1038/nsmb.1681