158l: Difference between revisions

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[[Image:158l.png|left|200px]]


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==CONTROL OF ENZYME ACTIVITY BY AN ENGINEERED DISULFIDE BOND==
The line below this paragraph, containing "STRUCTURE_158l", creates the "Structure Box" on the page.
<StructureSection load='158l' size='340' side='right'caption='[[158l]], [[Resolution|resolution]] 1.80&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'>[[158l]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_T4 Escherichia virus T4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=158L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=158L 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]] 1.8&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
{{STRUCTURE_158l| PDB=158l |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=158l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=158l OCA], [https://pdbe.org/158l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=158l RCSB], [https://www.ebi.ac.uk/pdbsum/158l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=158l ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ENLYS_BPT4 ENLYS_BPT4] Endolysin with lysozyme activity that degrades host peptidoglycans and participates with the holin and spanin proteins in the sequential events which lead to the programmed host cell lysis releasing the mature viral particles. Once the holin has permeabilized the host cell membrane, the endolysin can reach the periplasm and break down the peptidoglycan layer.<ref>PMID:22389108</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/58/158l_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=158l ConSurf].
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===CONTROL OF ENZYME ACTIVITY BY AN ENGINEERED DISULFIDE BOND===
==See Also==
 
*[[Lysozyme 3D structures|Lysozyme 3D structures]]
 
== References ==
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[[Category: Escherichia virus T4]]
{{ABSTRACT_PUBMED_7869383}}
[[Category: Large Structures]]
 
[[Category: Blaber M]]
==About this Structure==
[[Category: Matthews BW]]
158L is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_t4 Enterobacteria phage t4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=158L OCA].
 
==Reference==
<ref group="xtra">PMID:7869383</ref><references group="xtra"/>
[[Category: Enterobacteria phage t4]]
[[Category: Lysozyme]]
[[Category: Blaber, M.]]
[[Category: Matthews, B W.]]
 
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