256l: Difference between revisions

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New page: left|200px<br /><applet load="256l" size="450" color="white" frame="true" align="right" spinBox="true" caption="256l, resolution 1.8Å" /> '''BACTERIOPHAGE T4 LYSO...
 
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[[Image:256l.jpg|left|200px]]<br /><applet load="256l" size="450" color="white" frame="true" align="right" spinBox="true"
caption="256l, resolution 1.8&Aring;" />
'''BACTERIOPHAGE T4 LYSOZYME'''<br />


==Overview==
==BACTERIOPHAGE T4 LYSOZYME==
Phage T4 lysozyme consists of two domains between which is formed the, active-site cleft of the enzyme. The crystallographically determined, thermal displacement parameters for the protein suggested that the amino, terminal of the two domains undergoes 'hinge-bending' motion about an axis, passing through the waist of the molecule. Such conformational mobility, may be important in allowing access of substrates to the active site of, the enzyme. We report here a crystallographic study of a mutant T4, lysozyme which demonstrates further the conformational flexibility of the, protein. A mutant form of the enzyme with a methionine residue (Met 6), replaced by isoleucine crystallizes with four independent molecules in the, crystal lattice. These four molecules have distinctly different, conformations. The mutant protein can also crystallize in standard form, with a structure very similar to the wild-type protein. Thus the mutant, protein can adopt five different crystal conformations. The isoleucine for, methionine substitution at the intersection of the two domains of T4, lysozyme apparently enhances the hinge-bending motion presumed to occur in, the wild-type protein, without significantly affecting the catalytic, activity or thermal stability of the protein.
<StructureSection load='256l' size='340' side='right'caption='[[256l]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[256l]] 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=256L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=256L 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]] 1.8&#8491;</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=256l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=256l OCA], [https://pdbe.org/256l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=256l RCSB], [https://www.ebi.ac.uk/pdbsum/256l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=256l 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/56/256l_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=256l ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
256L is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_t4 Bacteriophage t4]. 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=256L OCA].
*[[Lysozyme 3D structures|Lysozyme 3D structures]]
 
== References ==
==Reference==
<references/>
A mutant T4 lysozyme displays five different crystal conformations., Faber HR, Matthews BW, Nature. 1990 Nov 15;348(6298):263-6. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=2234094 2234094]
__TOC__
[[Category: Bacteriophage t4]]
</StructureSection>
[[Category: Lysozyme]]
[[Category: Escherichia virus T4]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Faber, H.R.]]
[[Category: Faber HR]]
[[Category: Matthews, B.W.]]
[[Category: Matthews BW]]
[[Category: hydrolase]]
[[Category: lysozyme]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 07:50:12 2007''

Latest revision as of 12:09, 14 February 2024

BACTERIOPHAGE T4 LYSOZYMEBACTERIOPHAGE T4 LYSOZYME

Structural highlights

256l 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
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

256l, resolution 1.80Å

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