5i14
From Proteopedia
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<StructureSection load='5i14' size='340' side='right'caption='[[5i14]], [[Resolution|resolution]] 1.75Å' scene=''> | <StructureSection load='5i14' size='340' side='right'caption='[[5i14]], [[Resolution|resolution]] 1.75Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5i14]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[5i14]] is a 2 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=5I14 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5I14 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</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]] 1.745Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></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=5i14 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5i14 OCA], [https://pdbe.org/5i14 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5i14 RCSB], [https://www.ebi.ac.uk/pdbsum/5i14 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5i14 ProSAT]</span></td></tr> | ||
</table> | </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> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Escherichia virus T4]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Boura | + | [[Category: Boura E]] |
| - | [[Category: Klima | + | [[Category: Klima M]] |
| - | + | ||
| - | + | ||
Current revision
Truncated and mutated T4 lysozyme
<StructureSection load='5i14' size='340' side='right'caption='5i14, resolution 1.75Å' scene=>
Structural highlights
| 5i14 is a 2 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 1.745Å |
| Ligands: | <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene> |
| 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]
Publication Abstract from PubMed
Phage T4 lysozyme is a well folded and highly soluble protein that is widely used as an insertion tag to improve solubility and crystallization properties of poorly behaved recombinant proteins. It has been used in the fusion protein strategy to facilitate crystallization of various proteins including multiple G protein-coupled receptors, lipid kinases, or sterol binding proteins. Here, we present a structural and biochemical characterization of its novel, metal ions-binding mutant (mbT4L). We demonstrate that mbT4L can be used as a purification tag in the immobilized-metal affinity chromatography and that, in many respects, it is superior to the conventional hexahistidine tag. In addition, structural characterization of mbT4L suggests that mbT4L can be used as a purification tag compatible with X-ray crystallography.
Metal ions-binding T4 lysozyme as an intramolecular protein purification tag compatible with X-ray crystallography.,Boura E, Baumlova A, Chalupska D, Dubankova A, Klima M Protein Sci. 2017 Jun;26(6):1116-1123. doi: 10.1002/pro.3162. Epub 2017 Apr 2. PMID:28342173[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ 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
- ↑ Boura E, Baumlova A, Chalupska D, Dubankova A, Klima M. Metal ions-binding T4 lysozyme as an intramolecular protein purification tag compatible with X-ray crystallography. Protein Sci. 2017 Jun;26(6):1116-1123. doi: 10.1002/pro.3162. Epub 2017 Apr 2. PMID:28342173 doi:http://dx.doi.org/10.1002/pro.3162
Contents |
</StructureSection>
