1xjt
From Proteopedia
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| - | [[Image:1xjt.gif|left|200px]] | + | [[Image:1xjt.gif|left|200px]] |
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| - | '''Crystal structure of active form of P1 phage endolysin Lyz''' | + | {{Structure |
| + | |PDB= 1xjt |SIZE=350|CAPTION= <scene name='initialview01'>1xjt</scene>, resolution 1.750Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=CIT:CITRIC ACID'>CIT</scene> | ||
| + | |ACTIVITY= [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] | ||
| + | |GENE= 17, LYSA, lyZ ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10711 Enterobacteria phage P21]) | ||
| + | }} | ||
| + | |||
| + | '''Crystal structure of active form of P1 phage endolysin Lyz''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1XJT is a [ | + | 1XJT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_p21 Enterobacteria phage p21]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XJT OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15637279 15637279] |
[[Category: Enterobacteria phage p21]] | [[Category: Enterobacteria phage p21]] | ||
[[Category: Lysozyme]] | [[Category: Lysozyme]] | ||
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[[Category: open conformation]] | [[Category: open conformation]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:10:43 2008'' |
Revision as of 13:10, 20 March 2008
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| , resolution 1.750Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | 17, LYSA, lyZ (Enterobacteria phage P21) | ||||||
| Activity: | Lysozyme, with EC number 3.2.1.17 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of active 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
1XJT is a Single protein structure of sequence from Enterobacteria phage p21. 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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