189l

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{{Seed}}
 
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[[Image:189l.png|left|200px]]
 
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==ENHANCEMENT OF PROTEIN STABILITY BY THE COMBINATION OF POINT MUTATIONS IN T4 LYSOZYME IS ADDITIVE==
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The line below this paragraph, containing "STRUCTURE_189l", creates the "Structure Box" on the page.
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<StructureSection load='189l' size='340' side='right'caption='[[189l]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[189l]] 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=189L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=189L FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=189l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=189l OCA], [https://pdbe.org/189l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=189l RCSB], [https://www.ebi.ac.uk/pdbsum/189l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=189l ProSAT]</span></td></tr>
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{{STRUCTURE_189l| PDB=189l | SCENE= }}
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</table>
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/89/189l_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=189l ConSurf].
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<div style="clear:both"></div>
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===ENHANCEMENT OF PROTEIN STABILITY BY THE COMBINATION OF POINT MUTATIONS IN T4 LYSOZYME IS ADDITIVE===
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==See Also==
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*[[Lysozyme 3D structures|Lysozyme 3D structures]]
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== References ==
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The line below this paragraph, {{ABSTRACT_PUBMED_8771182}}, adds the Publication Abstract to the page
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__TOC__
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(as it appears on PubMed at http://www.pubmed.gov), where 8771182 is the PubMed ID number.
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</StructureSection>
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[[Category: Escherichia virus T4]]
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{{ABSTRACT_PUBMED_8771182}}
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[[Category: Large Structures]]
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[[Category: Matthews BW]]
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==About this Structure==
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[[Category: Zhang X-J]]
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189L 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=189L OCA].
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==Reference==
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<ref group="xtra">PMID:8771182</ref><references group="xtra"/>
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[[Category: Enterobacteria phage t4]]
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[[Category: Lysozyme]]
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[[Category: Matthews, B W.]]
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[[Category: Zhang, X J.]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 16:05:10 2009''
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Current revision

ENHANCEMENT OF PROTEIN STABILITY BY THE COMBINATION OF POINT MUTATIONS IN T4 LYSOZYME IS ADDITIVE

PDB ID 189l

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