4lzm: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
 
(10 intermediate revisions by the same user not shown)
Line 1: Line 1:
{{Seed}}
[[Image:4lzm.png|left|200px]]


<!--
==COMPARISON OF THE CRYSTAL STRUCTURE OF BACTERIOPHAGE T4 LYSOZYME AT LOW, MEDIUM, AND HIGH IONIC STRENGTHS==
The line below this paragraph, containing "STRUCTURE_4lzm", creates the "Structure Box" on the page.
<StructureSection load='4lzm' size='340' side='right'caption='[[4lzm]], [[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'>[[4lzm]] 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=4LZM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LZM 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>
-->
<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>
{{STRUCTURE_4lzm| PDB=4lzm |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4lzm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lzm OCA], [https://pdbe.org/4lzm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lzm RCSB], [https://www.ebi.ac.uk/pdbsum/4lzm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lzm 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/lz/4lzm_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=4lzm ConSurf].
<div style="clear:both"></div>


===COMPARISON OF THE CRYSTAL STRUCTURE OF BACTERIOPHAGE T4 LYSOZYME AT LOW, MEDIUM, AND HIGH IONIC STRENGTHS===
==See Also==
 
*[[Lysozyme 3D structures|Lysozyme 3D structures]]
 
== References ==
<!--
<references/>
The line below this paragraph, {{ABSTRACT_PUBMED_2062826}}, adds the Publication Abstract to the page
__TOC__
(as it appears on PubMed at http://www.pubmed.gov), where 2062826 is the PubMed ID number.
</StructureSection>
-->
[[Category: Escherichia virus T4]]
{{ABSTRACT_PUBMED_2062826}}
[[Category: Large Structures]]
 
[[Category: Bell JA]]
==About this Structure==
[[Category: Faber HR]]
4LZM 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=4LZM OCA].
[[Category: Matthews BW]]
 
[[Category: Nicholson H]]
==Reference==
[[Category: Wilson K]]
<ref group="xtra">PMID:2062826</ref><references group="xtra"/>
[[Category: Zhang X-J]]
[[Category: Enterobacteria phage t4]]
[[Category: Lysozyme]]
[[Category: Bell, J A.]]
[[Category: Faber, H R.]]
[[Category: Matthews, B W.]]
[[Category: Nicholson, H.]]
[[Category: Wilson, K.]]
[[Category: Zhang, X J.]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 15:28:44 2009''

Latest revision as of 15:22, 1 March 2024

COMPARISON OF THE CRYSTAL STRUCTURE OF BACTERIOPHAGE T4 LYSOZYME AT LOW, MEDIUM, AND HIGH IONIC STRENGTHSCOMPARISON OF THE CRYSTAL STRUCTURE OF BACTERIOPHAGE T4 LYSOZYME AT LOW, MEDIUM, AND HIGH IONIC STRENGTHS

Structural highlights

4lzm 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

4lzm, resolution 1.70Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA