2lc9: Difference between revisions

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[[Image:2lc9.png|left|200px]]


{{STRUCTURE_2lc9|  PDB=2lc9  |  SCENE=  }}
==Solution Structure of a Minor and Transiently Formed State of a T4 Lysozyme Mutant==
 
<StructureSection load='2lc9' size='340' side='right'caption='[[2lc9]]' scene=''>
===Solution Structure of a Minor and Transiently Formed State of a T4 Lysozyme Mutant===
== Structural highlights ==
 
<table><tr><td colspan='2'>[[2lc9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_T4 Escherichia virus T4]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LC9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LC9 FirstGlance]. <br>
{{ABSTRACT_PUBMED_21857680}}
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2lc9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lc9 OCA], [https://pdbe.org/2lc9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lc9 RCSB], [https://www.ebi.ac.uk/pdbsum/2lc9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lc9 ProSAT]</span></td></tr>
==About this Structure==
</table>
[[2lc9]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_t4 Enterobacteria phage t4]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LC9 OCA].  
== 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>


==See Also==
==See Also==
*[[Hen Egg-White (HEW) Lysozyme|Hen Egg-White (HEW) Lysozyme]]
*[[Lysozyme 3D structures|Lysozyme 3D structures]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:021857680</ref><references group="xtra"/>
__TOC__
[[Category: Enterobacteria phage t4]]
</StructureSection>
[[Category: Lysozyme]]
[[Category: Escherichia virus T4]]
[[Category: Bah, A.]]
[[Category: Large Structures]]
[[Category: Baker, D.]]
[[Category: Bah A]]
[[Category: Bouvignies, G.]]
[[Category: Baker D]]
[[Category: Correia, B.]]
[[Category: Bouvignies G]]
[[Category: Dahlquist, F W.]]
[[Category: Correia B]]
[[Category: Hansen, D.]]
[[Category: Dahlquist FW]]
[[Category: Kay, L E.]]
[[Category: Hansen D]]
[[Category: Lange, O.]]
[[Category: Kay LE]]
[[Category: Vallurupalli, P.]]
[[Category: Lange O]]
[[Category: Vernon, R M.]]
[[Category: Vallurupalli P]]
[[Category: Hydrolase]]
[[Category: Vernon RM]]

Latest revision as of 09:55, 1 May 2024

Solution Structure of a Minor and Transiently Formed State of a T4 Lysozyme MutantSolution Structure of a Minor and Transiently Formed State of a T4 Lysozyme Mutant

Structural highlights

2lc9 is a 1 chain structure with sequence from Escherichia virus T4. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
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
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