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[[Image:103l.gif|left|200px]]<br />
<applet load="103l" size="450" color="white" frame="true" align="right" spinBox="true"
caption="103l, resolution 1.9&Aring;" />
'''HOW AMINO-ACID INSERTIONS ARE ALLOWED IN AN ALPHA-HELIX OF T4 LYSOZYME'''<br />


==Overview==
==HOW AMINO-ACID INSERTIONS ARE ALLOWED IN AN ALPHA-HELIX OF T4 LYSOZYME==
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 ways. In some cases the inserted amino acids are, accommodated within the helix, leading to the translocation of wild-type, residues from the helix to the preceding loop. In other cases the, insertion causes a 'looping-out' in the first or last turn of the helix., The individual structural responses seem to be dominated by the, maintenance of the interface between the helix and the rest of the, protein.
<StructureSection load='103l' size='340' side='right'caption='[[103l]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[103l]] 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=103L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=103L FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
<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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=103l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=103l OCA], [https://pdbe.org/103l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=103l RCSB], [https://www.ebi.ac.uk/pdbsum/103l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=103l 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/03/103l_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=103l ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
103L is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_t2 Enterobacteria phage t2] 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=103L OCA].
*[[Lysozyme 3D structures|Lysozyme 3D structures]]
 
== References ==
==Reference==
<references/>
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]
__TOC__
[[Category: Enterobacteria phage t2]]
</StructureSection>
[[Category: Single protein]]
[[Category: Escherichia virus T4]]
[[Category: Heinz, D.W.]]
[[Category: Large Structures]]
[[Category: Matthews, B.W.]]
[[Category: Heinz DW]]
[[Category: BME]]
[[Category: Matthews BW]]
[[Category: CL]]
[[Category: hydrolase(o-glycosyl)]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 15:49:44 2007''

Latest revision as of 09:23, 7 February 2024

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

Structural highlights

103l is a 1 chain structure with sequence from Escherichia virus T4. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.9Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Moussa SH, Kuznetsov V, Tran TA, Sacchettini JC, Young R. Protein determinants of phage T4 lysis inhibition. Protein Sci. 2012 Apr;21(4):571-82. doi: 10.1002/pro.2042. Epub 2012 Mar 2. PMID:22389108 doi:http://dx.doi.org/10.1002/pro.2042

103l, resolution 1.90Å

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