1xju
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(New page: 200px<br /><applet load="1xju" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xju, resolution 1.070Å" /> '''Crystal structure o...)
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Revision as of 03:59, 21 November 2007
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Crystal structure of secreted inactive form of P1 phage endolysin Lyz
Overview
The P1 lysozyme Lyz is secreted to the periplasm of Escherichia coli and, accumulates in an inactive membrane-tethered form. Genetic and biochemical, experiments show that, when released from the bilayer, Lyz is activated by, an intramolecular thiol-disulfide isomerization, which requires a cysteine, in its N-terminal SAR (signal-arrest-release) domain. Crystal structures, confirm the alternative disulfide linkages in the two forms of Lyz and, reveal dramatic conformational differences in the catalytic domain. Thus, the exported P1 endolysin is kept inactive by three levels of, control-topological, conformational, and covalent-until its release from, the membrane is triggered by the P1 holin.
About this Structure
1XJU is a Single protein structure of sequence from Enterobacteria phage p21 with SO4 as ligand. Active as Lysozyme, with EC number 3.2.1.17 Full crystallographic information is available from OCA.
Reference
Disulfide isomerization after membrane release of its SAR domain activates P1 lysozyme., Xu M, Arulandu A, Struck DK, Swanson S, Sacchettini JC, Young R, Science. 2005 Jan 7;307(5706):113-7. PMID:15637279
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