232l: Difference between revisions

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New page: left|200px<br /><applet load="232l" size="450" color="white" frame="true" align="right" spinBox="true" caption="232l, resolution 1.73Å" /> '''T4 LYSOZYME MUTANT M...
 
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[[Image:232l.jpg|left|200px]]<br /><applet load="232l" size="450" color="white" frame="true" align="right" spinBox="true"
caption="232l, resolution 1.73&Aring;" />
'''T4 LYSOZYME MUTANT M120K'''<br />


==Overview==
==T4 LYSOZYME MUTANT M120K==
The substitution of methionines with leucines within the interior of a, protein is expected to increase stability both because of a more favorable, solvent transfer term as well as the reduced entropic cost of holding a, leucine side chain in a defined position. Together, these two terms are, expected to contribute about 1.4 kcal/mol to protein stability for each, Met --&gt; Leu substitution when fully buried. At the same time, this, expected beneficial effect may be offset by steric factors due to, differences in the shape of leucine and methionine. To investigate the, interplay between these factors, all methionines in T4 lysozyme except at, the amino-terminus were individually replaced with leucine. Of these, mutants, M106L and M120L have stabilities 0.5 kcal/mol higher than, wild-type T4 lysozyme, while M6L is significantly destabilized (-2.8, kcal/mol). M102L, described previously, is also destabilized (-0.9, kcal/mol). Based on this limited sample it appears that, methionine-to-leucine substitutions can increase protein stability but, only in a situation where the methionine side chain is fully or partially, buried, yet allows the introduction of the leucine without concomitant, steric interference. The variants, together with methionine-to-lysine, substitutions at the same sites, follow the general pattern that, substitutions at rigid, internal sites tend to be most destabilizing, whereas replacements at more solvent-exposed sites are better tolerated.
<StructureSection load='232l' size='340' side='right'caption='[[232l]], [[Resolution|resolution]] 1.73&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[232l]] 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=232L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=232L 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]] 1.73&#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=232l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=232l OCA], [https://pdbe.org/232l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=232l RCSB], [https://www.ebi.ac.uk/pdbsum/232l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=232l 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/32/232l_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=232l ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
232L is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_t4 Bacteriophage t4] with CL and BME as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=232L OCA].
*[[Lysozyme 3D structures|Lysozyme 3D structures]]
 
== References ==
==Reference==
<references/>
Context-dependent protein stabilization by methionine-to-leucine substitution shown in T4 lysozyme., Lipscomb LA, Gassner NC, Snow SD, Eldridge AM, Baase WA, Drew DL, Matthews BW, Protein Sci. 1998 Mar;7(3):765-73. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9541409 9541409]
__TOC__
[[Category: Bacteriophage t4]]
</StructureSection>
[[Category: Lysozyme]]
[[Category: Escherichia virus T4]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Baase, W.A.]]
[[Category: Baase WA]]
[[Category: Drew, D.L.]]
[[Category: Drew DL]]
[[Category: Gassner, N.]]
[[Category: Gassner N]]
[[Category: Lipscomb, L.A.]]
[[Category: Lipscomb LA]]
[[Category: Matthews, B.W.]]
[[Category: Matthews BW]]
[[Category: BME]]
[[Category: CL]]
[[Category: glycosidase]]
[[Category: hydrolase]]
[[Category: o-glycosyl]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 07:48:16 2007''

Latest revision as of 12:08, 14 February 2024

T4 LYSOZYME MUTANT M120KT4 LYSOZYME MUTANT M120K

Structural highlights

232l 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 1.73Å
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

232l, resolution 1.73Å

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