1xju

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (07:37, 30 October 2024) (edit) (undo)
 
(11 intermediate revisions not shown.)
Line 1: Line 1:
-
{{Seed}}
 
-
[[Image:1xju.png|left|200px]]
 
-
<!--
+
==Crystal structure of secreted inactive form of P1 phage endolysin Lyz==
-
The line below this paragraph, containing "STRUCTURE_1xju", creates the "Structure Box" on the page.
+
<StructureSection load='1xju' size='340' side='right'caption='[[1xju]], [[Resolution|resolution]] 1.07&Aring;' scene=''>
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
== Structural highlights ==
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
<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>
-
or leave the SCENE parameter empty for the default display.
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.07&#8491;</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>
-
{{STRUCTURE_1xju| PDB=1xju | SCENE= }}
+
<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.
-
===Crystal structure of secreted inactive form of P1 phage endolysin Lyz===
+
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>
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 1xju" style="background-color:#fffaf0;"></div>
-
<!--
+
==See Also==
-
The line below this paragraph, {{ABSTRACT_PUBMED_15637279}}, adds the Publication Abstract to the page
+
*[[Lysozyme 3D structures|Lysozyme 3D structures]]
-
(as it appears on PubMed at http://www.pubmed.gov), where 15637279 is the PubMed ID number.
+
== References ==
-
-->
+
<references/>
-
{{ABSTRACT_PUBMED_15637279}}
+
__TOC__
-
 
+
</StructureSection>
-
==About this Structure==
+
[[Category: Escherichia virus P1]]
-
1XJU is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_p1 Enterobacteria phage p1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XJU OCA].
+
[[Category: Large Structures]]
-
 
+
[[Category: Arockiasamy A]]
-
==Reference==
+
[[Category: Sacchettini JC]]
-
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 p1]]
+
-
[[Category: Lysozyme]]
+
-
[[Category: Single protein]]
+
-
[[Category: Arockiasamy, A.]]
+
-
[[Category: Sacchettini, J C.]]
+
-
[[Category: Secreted inactive conformation]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 21:56:23 2008''
+

Current revision

Crystal structure of secreted inactive form of P1 phage endolysin Lyz

PDB ID 1xju

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1xju"
Personal tools