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[[Image:1qt7.jpg|left|200px]]


{{Structure
==E11N Mutant of T4 Lysozyme==
|PDB= 1qt7 |SIZE=350|CAPTION= <scene name='initialview01'>1qt7</scene>, resolution 1.8&Aring;
<StructureSection load='1qt7' size='340' side='right'caption='[[1qt7]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> and <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>
<table><tr><td colspan='2'>[[1qt7]] 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=1QT7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QT7 FirstGlance]. <br>
|ACTIVITY= [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]  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
|GENE=  
<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=1qt7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qt7 OCA], [https://pdbe.org/1qt7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qt7 RCSB], [https://www.ebi.ac.uk/pdbsum/1qt7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qt7 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/qt/1qt7_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=1qt7 ConSurf].
<div style="clear:both"></div>


'''E11N Mutant of T4 Lysozyme'''
==See Also==
 
*[[Lysozyme 3D structures|Lysozyme 3D structures]]
 
== References ==
==Overview==
<references/>
In contrast to hen egg-white lysozyme, which retains the beta-configuration of the substrate in the product, T4 lysozyme (T4L) is an inverting glycosidase. The substitution Thr-26 --&gt; His, however, converts T4L from an inverting to a retaining enzyme. It is shown here that the Thr-26 --&gt; His mutant is also a transglycosidase. Indeed, the transglycosylation reaction can be more effective than hydrolysis. In contrast, wild-type T4L has no detectable transglycosidase activity. The results support the prior hypothesis that catalysis by the Thr-26 --&gt; His mutant proceeds via a covalent intermediate. Further mutations (Glu-11 --&gt; His, Asp-20 --&gt; Cys) of the T26H mutant lysozyme indicate that the catalytic mechanism of this mutant requires Glu-11 as a general acid but Asp-20 is not essential. The results help provide an overall rationalization for the activity of glycosidases, in which a highly conserved acid group (Glu-11 in T4L, Glu-35 in hen egg-white lysozyme) on the beta-side of the substrate acts as a proton donor, whereas alterations in the placement and chemical identity of residues on the alpha-side of the substrate can lead to catalysis with or without retention of the configuration, to transglycosidase activity, or to the formation of a stable enzyme-substrate adduct.
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Escherichia virus T4]]
1QT7 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_phage_d3112 Pseudomonas phage d3112]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QT7 OCA].
[[Category: Large Structures]]
 
[[Category: Kuroki R]]
==Reference==
[[Category: Matthews BW]]
Structural basis of the conversion of T4 lysozyme into a transglycosidase by reengineering the active site., Kuroki R, Weaver LH, Matthews BW, Proc Natl Acad Sci U S A. 1999 Aug 3;96(16):8949-54. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10430876 10430876]
[[Category: Weaver LH]]
[[Category: Lysozyme]]
[[Category: Pseudomonas phage d3112]]
[[Category: Single protein]]
[[Category: Kuroki, R.]]
[[Category: Matthews, B W.]]
[[Category: Weaver, L H.]]
[[Category: BME]]
[[Category: CL]]
[[Category: hydrolase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:42:23 2008''

Latest revision as of 11:17, 14 February 2024

E11N Mutant of T4 LysozymeE11N Mutant of T4 Lysozyme

Structural highlights

1qt7 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 1.8Å
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

1qt7, resolution 1.80Å

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