1xju
From Proteopedia
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| - | [[Image:1xju.gif|left|200px]] | ||
| - | + | ==Crystal structure of secreted inactive form of P1 phage endolysin Lyz== | |
| - | + | <StructureSection load='1xju' size='340' side='right'caption='[[1xju]], [[Resolution|resolution]] 1.07Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | | | + | <table><tr><td colspan='2'>[[1xju]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_P1 Escherichia virus P1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XJU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XJU FirstGlance]. <br> |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.07Å</td></tr> | |
| - | | | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1xju FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xju OCA], [https://pdbe.org/1xju PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xju RCSB], [https://www.ebi.ac.uk/pdbsum/1xju PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xju ProSAT]</span></td></tr> | |
| - | + | </table> | |
| - | + | == Function == | |
| - | + | [https://www.uniprot.org/uniprot/ENLYS_BPP1 ENLYS_BPP1] Signal-arrest-release (SAR) endolysin with lysozyme activity that degrades host peptidoglycans and participates with the pinholin and spanin proteins in the sequential events which lead to programmed host cell lysis releasing the mature viral particles. Once the pinholin has permeabilized the host cell membrane, the SAR-endolysin is released into the periplasm where it breaks down the peptidoglycan layer.[HAMAP-Rule:MF_04136]<ref>PMID:15090650</ref> | |
| - | + | == Evolutionary Conservation == | |
| - | == | + | [[Image:Consurf_key_small.gif|200px|right]] |
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/xj/1xju_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1xju ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
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. | 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. | ||
| - | + | 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<ref>PMID:15637279</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 1xju" style="background-color:#fffaf0;"></div> | |
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| - | + | ==See Also== | |
| + | *[[Lysozyme 3D structures|Lysozyme 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Escherichia virus P1]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Arockiasamy A]] | ||
| + | [[Category: Sacchettini JC]] | ||
Current revision
Crystal structure of secreted inactive form of P1 phage endolysin Lyz
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