1l02: Difference between revisions

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{{Seed}}
[[Image:1l02.png|left|200px]]


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==CONTRIBUTIONS OF HYDROGEN BONDS OF THR 157 TO THE THERMODYNAMIC STABILITY OF PHAGE T4 LYSOZYME==
The line below this paragraph, containing "STRUCTURE_1l02", creates the "Structure Box" on the page.
<StructureSection load='1l02' size='340' side='right'caption='[[1l02]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1l02]] 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=1L02 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1L02 FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1l02 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l02 OCA], [https://pdbe.org/1l02 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1l02 RCSB], [https://www.ebi.ac.uk/pdbsum/1l02 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1l02 ProSAT]</span></td></tr>
{{STRUCTURE_1l02|  PDB=1l02  |  SCENE= }}
</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/l0/1l02_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=1l02 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Measurements of changes in structure and stability caused by 13 different substitutions for threonine 157 in phage T4 lysozyme show that the most stable lysozyme variants contain hydrogen bonds analogous to those in the wild-type enzyme and that structural adjustments allow the protein to be surprisingly tolerant of amino-acid substitutions.


===CONTRIBUTIONS OF HYDROGEN BONDS OF THR 157 TO THE THERMODYNAMIC STABILITY OF PHAGE T4 LYSOZYME===
Contributions of hydrogen bonds of Thr 157 to the thermodynamic stability of phage T4 lysozyme.,Alber T, Sun DP, Wilson K, Wozniak JA, Cook SP, Matthews BW Nature. 1987 Nov 5-11;330(6143):41-6. PMID:3118211<ref>PMID:3118211</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1l02" style="background-color:#fffaf0;"></div>


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==See Also==
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*[[Lysozyme 3D structures|Lysozyme 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 3118211 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_3118211}}
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</StructureSection>
==About this Structure==
[[Category: Escherichia virus T4]]
1L02 is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_t4 Enterobacteria phage t4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L02 OCA].
[[Category: Large Structures]]
 
[[Category: Alber T]]
==Reference==
[[Category: Dao-Pin S]]
<ref group="xtra">PMID:3118211</ref><references group="xtra"/>
[[Category: Matthews BW]]
[[Category: Enterobacteria phage t4]]
[[Category: Lysozyme]]
[[Category: Alber, T.]]
[[Category: Dao-Pin, S.]]
[[Category: Matthews, B W.]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 04:12:11 2009''

Latest revision as of 11:43, 22 May 2024

CONTRIBUTIONS OF HYDROGEN BONDS OF THR 157 TO THE THERMODYNAMIC STABILITY OF PHAGE T4 LYSOZYMECONTRIBUTIONS OF HYDROGEN BONDS OF THR 157 TO THE THERMODYNAMIC STABILITY OF PHAGE T4 LYSOZYME

Structural highlights

1l02 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
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.

Publication Abstract from PubMed

Measurements of changes in structure and stability caused by 13 different substitutions for threonine 157 in phage T4 lysozyme show that the most stable lysozyme variants contain hydrogen bonds analogous to those in the wild-type enzyme and that structural adjustments allow the protein to be surprisingly tolerant of amino-acid substitutions.

Contributions of hydrogen bonds of Thr 157 to the thermodynamic stability of phage T4 lysozyme.,Alber T, Sun DP, Wilson K, Wozniak JA, Cook SP, Matthews BW Nature. 1987 Nov 5-11;330(6143):41-6. PMID:3118211[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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
  2. ↑ Alber T, Sun DP, Wilson K, Wozniak JA, Cook SP, Matthews BW. Contributions of hydrogen bonds of Thr 157 to the thermodynamic stability of phage T4 lysozyme. Nature. 1987 Nov 5-11;330(6143):41-6. PMID:3118211 doi:http://dx.doi.org/10.1038/330041a0

1l02, resolution 1.70Å

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