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==Crystal Structure of Spin Labeled T4 Lysozyme Mutant 115-119RX==
==Crystal Structure of Spin Labeled T4 Lysozyme Mutant 115-119RX==
<StructureSection load='3l2x' size='340' side='right' caption='[[3l2x]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='3l2x' size='340' side='right'caption='[[3l2x]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3l2x]] is a 1 chain structure with 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=3L2X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3L2X FirstGlance]. <br>
<table><tr><td colspan='2'>[[3l2x]] 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=3L2X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3L2X FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AZI:AZIDE+ION'>AZI</scene>, <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=HED:2-HYDROXYETHYL+DISULFIDE'>HED</scene>, <scene name='pdbligand=RXR:[2,2,5,5-TETRAMETHYL-3,4-BIS(SULFANYLMETHYL)-2,5-DIHYDRO-1H-PYRROL-1-YL]OXIDANYL+RADICAL'>RXR</scene></td></tr>
</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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">E, Lysozyme ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10665 Enterobacteria phage T4])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AZI:AZIDE+ION'>AZI</scene>, <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=HED:2-HYDROXYETHYL+DISULFIDE'>HED</scene>, <scene name='pdbligand=RXR:[2,2,5,5-TETRAMETHYL-3,4-BIS(SULFANYLMETHYL)-2,5-DIHYDRO-1H-PYRROL-1-YL]OXIDANYL+RADICAL'>RXR</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></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=3l2x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3l2x OCA], [https://pdbe.org/3l2x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3l2x RCSB], [https://www.ebi.ac.uk/pdbsum/3l2x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3l2x ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3l2x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3l2x OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3l2x RCSB], [http://www.ebi.ac.uk/pdbsum/3l2x PDBsum]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/LYS_BPT4 LYS_BPT4]] Helps to release the mature phage particles from the cell wall by breaking down the peptidoglycan.  
[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>


==See Also==
==See Also==
*[[Lysozyme 3D structures|Lysozyme 3D structures]]
*[[Lysozyme 3D structures|Lysozyme 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Enterobacteria phage t4]]
[[Category: Escherichia virus T4]]
[[Category: Lysozyme]]
[[Category: Large Structures]]
[[Category: Cascio, D]]
[[Category: Cascio D]]
[[Category: Fleissner, M R]]
[[Category: Fleissner MR]]
[[Category: Hubbell, W L]]
[[Category: Hubbell WL]]
[[Category: Antimicrobial]]
[[Category: Bacteriolytic enzyme]]
[[Category: Epr]]
[[Category: Glycosidase]]
[[Category: Hydrolase]]
[[Category: Modified cysteine]]
[[Category: Nitroxide spin label]]

Latest revision as of 09:35, 19 July 2023

Crystal Structure of Spin Labeled T4 Lysozyme Mutant 115-119RXCrystal Structure of Spin Labeled T4 Lysozyme Mutant 115-119RX

Structural highlights

3l2x 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]

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

3l2x, resolution 1.80Å

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