1xju
From Proteopedia
(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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| - | [[Image:1xju.gif|left|200px]]<br /><applet load="1xju" size=" | + | [[Image:1xju.gif|left|200px]]<br /><applet load="1xju" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1xju, resolution 1.070Å" /> | caption="1xju, resolution 1.070Å" /> | ||
'''Crystal structure of secreted inactive form of P1 phage endolysin Lyz'''<br /> | '''Crystal structure of secreted inactive form of P1 phage endolysin Lyz'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The P1 lysozyme Lyz is secreted to the periplasm of Escherichia coli and | + | 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== | ==About this Structure== | ||
| - | 1XJU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_p21 Enterobacteria phage p21] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] Full crystallographic information is available from [http:// | + | 1XJU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_p21 Enterobacteria phage p21] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XJU OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Arockiasamy, A.]] | [[Category: Arockiasamy, A.]] | ||
| - | [[Category: Sacchettini, J | + | [[Category: Sacchettini, J C.]] |
[[Category: SO4]] | [[Category: SO4]] | ||
[[Category: secreted inactive conformation]] | [[Category: secreted inactive conformation]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:55:30 2008'' |
Revision as of 13:55, 21 February 2008
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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 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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