131l: Difference between revisions

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New page: left|200px<br /><applet load="131l" size="450" color="white" frame="true" align="right" spinBox="true" caption="131l, resolution 1.7Å" /> '''STRUCTURES OF RANDOML...
 
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[[Image:131l.jpg|left|200px]]<br /><applet load="131l" size="450" color="white" frame="true" align="right" spinBox="true"
caption="131l, resolution 1.7&Aring;" />
'''STRUCTURES OF RANDOMLY GENERATED MUTANTS OF T4 LYSOZYME SHOW THAT PROTEIN STABILITY CAN BE ENHANCED BY RELAXATION OF STRAIN AND BY IMPROVED HYDROGEN BONDING VIA BOUND SOLVENT'''<br />


==Overview==
==STRUCTURES OF RANDOMLY GENERATED MUTANTS OF T4 LYSOZYME SHOW THAT PROTEIN STABILITY CAN BE ENHANCED BY RELAXATION OF STRAIN AND BY IMPROVED HYDROGEN BONDING VIA BOUND SOLVENT==
The structures of three mutants of bacteriophage T4 lysozyme selected, using a screen designed to identify thermostable variants are described., Each of the mutants has a substitution involving threonine. Two of the, variants, Thr 26--&gt;Ser (T26S) and Thr 151--&gt;Ser (T151S), have increased, reversible melting temperatures with respect to the wild-type protein. The, third, Ala 93--&gt;Thr (A93T), has essentially the same stability as wild, type. Thr 26 is in the wall of the active-site cleft. Its replacement with, serine results in the rearrangement of nearby residues, most notably Tyr, 18, suggesting that the increase in stability may result from the removal, of strain. Thr 151 in the wild-type structure is far from the active site, and appears to sterically prevent the access of solvent to a preformed, binding site. In the mutant, the removal of the methyl group allows access, to the solvent binding site and, in addition, the Ser 151 hydroxyl rotates, to a new position so that it also contributes to solvent binding. Residue, 93 is in a highly exposed site on the surface of the molecule, and, presumably is equally solvent exposed in the unfolded protein. It is, therefore, not surprising that the substitution Ala 93--&gt;Thr does not, change stability. The mutant structures show how chemically similar, mutations can have different effects on both the structure and stability, of the protein, depending on the structural context. The results also, illustrate the power of random mutagenesis in obtaining variants with a, desired phenotype.(ABSTRACT TRUNCATED AT 250 WORDS)
<StructureSection load='131l' size='340' side='right'caption='[[131l]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[131l]] 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=131L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=131L 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]] 1.7&#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=131l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=131l OCA], [https://pdbe.org/131l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=131l RCSB], [https://www.ebi.ac.uk/pdbsum/131l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=131l 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/31/131l_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=131l ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
131L 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]. 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=131L OCA].
*[[Lysozyme 3D structures|Lysozyme 3D structures]]
 
== References ==
==Reference==
<references/>
Structures of randomly generated mutants of T4 lysozyme show that protein stability can be enhanced by relaxation of strain and by improved hydrogen bonding via bound solvent., Pjura P, Matthews BW, Protein Sci. 1993 Dec;2(12):2226-32. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8298466 8298466]
__TOC__
[[Category: Enterobacteria phage t2]]
</StructureSection>
[[Category: Lysozyme]]
[[Category: Escherichia virus T4]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Matthews, B.W.]]
[[Category: Matthews BW]]
[[Category: Pjura, P.]]
[[Category: Pjura P]]
[[Category: BME]]
[[Category: CL]]
[[Category: hydrolase(o-glycosyl)]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 10:26:34 2007''

Latest revision as of 09:24, 7 February 2024

STRUCTURES OF RANDOMLY GENERATED MUTANTS OF T4 LYSOZYME SHOW THAT PROTEIN STABILITY CAN BE ENHANCED BY RELAXATION OF STRAIN AND BY IMPROVED HYDROGEN BONDING VIA BOUND SOLVENTSTRUCTURES OF RANDOMLY GENERATED MUTANTS OF T4 LYSOZYME SHOW THAT PROTEIN STABILITY CAN BE ENHANCED BY RELAXATION OF STRAIN AND BY IMPROVED HYDROGEN BONDING VIA BOUND SOLVENT

Structural highlights

131l 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 1.7Å
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

131l, resolution 1.70Å

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