102l

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(New page: 200px<br /> <applet load="102l" size="450" color="white" frame="true" align="right" spinBox="true" caption="102l, resolution 1.74&Aring;" /> '''HOW AMINO-ACID INSE...)
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[[Image:102l.gif|left|200px]]<br />
 
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<applet load="102l" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="102l, resolution 1.74&Aring;" />
 
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'''HOW AMINO-ACID INSERTIONS ARE ALLOWED IN AN ALPHA-HELIX OF T4 LYSOZYME'''<br />
 
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==Overview==
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==HOW AMINO-ACID INSERTIONS ARE ALLOWED IN AN ALPHA-HELIX OF T4 LYSOZYME==
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Studies of extant protein sequences indicate that amino-acid insertions, and deletions are preferentially located in loop regions, which has, traditionally been explained as the result of selection removing, deleterious mutations within secondary structural elements from the, population. But there is no a priori reason to discount the possibility, that insertions within secondary structure could either be tolerated until, compensatory mutations arise, or have effects that are propagated away, from secondary structure into loops. Earlier studies have indicated that, insertions are generally tolerated, although much less well within, secondary structure elements than in loop regions. Here we show that, amino-acid insertions in an alpha-helix of T4 lysozyme can be accepted in, two different ... [[http://ispc.weizmann.ac.il/pmbin/getpm?8429913 (full description)]]
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<StructureSection load='102l' size='340' side='right'caption='[[102l]], [[Resolution|resolution]] 1.74&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[102l]] 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=102L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=102L FirstGlance]. <br>
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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]] 1.74&#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>
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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=102l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=102l OCA], [https://pdbe.org/102l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=102l RCSB], [https://www.ebi.ac.uk/pdbsum/102l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=102l ProSAT]</span></td></tr>
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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/02/102l_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=102l ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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102L is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Coliphage_t4 Coliphage t4]] with CL and BME as [[http://en.wikipedia.org/wiki/ligands ligands]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id= OCA]].
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*[[Lysozyme 3D structures|Lysozyme 3D structures]]
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== References ==
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==Reference==
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<references/>
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How amino-acid insertions are allowed in an alpha-helix of T4 lysozyme., Heinz DW, Baase WA, Dahlquist FW, Matthews BW, Nature. 1993 Feb 11;361(6412):561-4. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8429913 8429913]
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__TOC__
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[[Category: Coliphage t4]]
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</StructureSection>
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[[Category: Single protein]]
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[[Category: Escherichia virus T4]]
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[[Category: Heinz, D.W.]]
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[[Category: Large Structures]]
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[[Category: Matthews, B.W.]]
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[[Category: Heinz DW]]
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[[Category: BME]]
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[[Category: Matthews BW]]
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[[Category: CL]]
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[[Category: hydrolase(o-glycosyl)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 15:37:51 2007''
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Current revision

HOW AMINO-ACID INSERTIONS ARE ALLOWED IN AN ALPHA-HELIX OF T4 LYSOZYME

PDB ID 102l

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