216l

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{{Seed}}
 
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[[Image:216l.png|left|200px]]
 
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==STRUCTURAL BASIS OF ALPHA-HELIX PROPENSITY AT TWO SITES IN T4 LYSOZYME==
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The line below this paragraph, containing "STRUCTURE_216l", creates the "Structure Box" on the page.
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<StructureSection load='216l' size='340' side='right'caption='[[216l]], [[Resolution|resolution]] 2.10&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'>[[216l]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_T4 Escherichia virus T4]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=116l 116l]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=216L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=216L 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]] 2.1&#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=216l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=216l OCA], [https://pdbe.org/216l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=216l RCSB], [https://www.ebi.ac.uk/pdbsum/216l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=216l ProSAT]</span></td></tr>
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{{STRUCTURE_216l| PDB=216l | 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/16/216l_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=216l ConSurf].
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<div style="clear:both"></div>
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===STRUCTURAL BASIS OF ALPHA-HELIX PROPENSITY AT TWO SITES IN T4 LYSOZYME===
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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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<references/>
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__TOC__
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(as it appears on PubMed at http://www.pubmed.gov), where 8503008 is the PubMed ID number.
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</StructureSection>
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[[Category: Escherichia virus T4]]
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{{ABSTRACT_PUBMED_8503008}}
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[[Category: Large Structures]]
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[[Category: Blaber M]]
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==About this Structure==
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[[Category: Matthews BW]]
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216L is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Enterobacteria_phage_t4 Enterobacteria phage t4]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=116l 116l]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=216L OCA].
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==Reference==
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<ref group="xtra">PMID:8503008</ref><references group="xtra"/>
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[[Category: Enterobacteria phage t4]]
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[[Category: Lysozyme]]
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[[Category: Blaber, M.]]
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[[Category: Matthews, B W.]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 05:17:07 2009''
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Current revision

STRUCTURAL BASIS OF ALPHA-HELIX PROPENSITY AT TWO SITES IN T4 LYSOZYME

PDB ID 216l

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