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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.

SUBMITTER: Sun Q 

PROVIDER: S-EPMC3075974 | biostudies-literature | 2009 Nov

REPOSITORIES: biostudies-literature

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Regulation of a muralytic enzyme by dynamic membrane topology.

Sun Qingan Q   Kuty Gabriel F GF   Arockiasamy Arulandu A   Xu Min M   Young Ry R   Sacchettini James C JC  

Nature structural & molecular biology 20091101 11


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. ...[more]

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