1xju

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{{STRUCTURE_1xju| PDB=1xju | SCENE= }}
{{STRUCTURE_1xju| PDB=1xju | SCENE= }}
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'''Crystal structure of secreted inactive form of P1 phage endolysin Lyz'''
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===Crystal structure of secreted inactive form of P1 phage endolysin Lyz===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 15637279 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15637279}}
==About this Structure==
==About this Structure==
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[[Category: Sacchettini, J C.]]
[[Category: Sacchettini, J C.]]
[[Category: Secreted inactive conformation]]
[[Category: Secreted inactive conformation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 21:56:23 2008''

Revision as of 18:56, 28 July 2008

Image:1xju.png

Template:STRUCTURE 1xju

Crystal structure of secreted inactive form of P1 phage endolysin Lyz

Template:ABSTRACT PUBMED 15637279

About this Structure

1XJU is a Single protein structure of sequence from Enterobacteria phage p1. 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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