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| | <StructureSection load='1jtn' size='340' side='right'caption='[[1jtn]], [[Resolution|resolution]] 2.30Å' scene=''> | | <StructureSection load='1jtn' size='340' side='right'caption='[[1jtn]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1jtn]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bpt4 Bpt4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JTN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JTN FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1jtn]] 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=1JTN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JTN FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.3Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1jtm|1jtm]]</div></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">E ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10665 BPT4])</td></tr> | + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [https://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=1jtn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jtn OCA], [https://pdbe.org/1jtn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jtn RCSB], [https://www.ebi.ac.uk/pdbsum/1jtn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jtn ProSAT]</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=1jtn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jtn OCA], [https://pdbe.org/1jtn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jtn RCSB], [https://www.ebi.ac.uk/pdbsum/1jtn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jtn ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://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> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bpt4]] | + | [[Category: Escherichia virus T4]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lysozyme]]
| + | [[Category: Matthews BW]] |
| - | [[Category: Matthews, B W]] | + | [[Category: Sagermann M]] |
| - | [[Category: Sagermann, M]] | + | |
| - | [[Category: Context dependent folding]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Sequence duplication]]
| + | |
| - | [[Category: Sequence repeat]]
| + | |
| Structural highlights
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
Residues 24 to 35 of T4 lysozyme correspond to the second and third strands of a region of beta-sheet that is highly conserved in all known lysozyme and chitinase structures. To evaluate the intrinsic propensity of these amino acid residues to form a defined structure they were added at the C terminus of the native protein, together with a dipeptide linker. Two crystal structures of this active, mutant protein were obtained, to 1.9A and 2.3A resolution, respectively. Even though the crystal conditions are similar, the appended sequence adopts very different secondary structures. In one case it is weakly structured and appears to extend through the active-site cleft, perhaps in part adding an extra strand to the original beta-sheet. In the other crystal form the extension is largely alpha-helical. The formation of these alternative structures shows that the sequence does not have a strong intrinsic propensity to form a unique fold (either beta-sheet or otherwise). The results also suggest that structural conservation during evolution does not necessarily depend on sequence conservation or the conservation of folding propensity.
Crystal structures of a T4-lysozyme duplication-extension mutant demonstrate that the highly conserved beta-sheet region has low intrinsic folding propensity.,Sagermann M, Matthews BW J Mol Biol. 2002 Mar 1;316(4):931-40. PMID:11884133[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
- ↑ Sagermann M, Matthews BW. Crystal structures of a T4-lysozyme duplication-extension mutant demonstrate that the highly conserved beta-sheet region has low intrinsic folding propensity. J Mol Biol. 2002 Mar 1;316(4):931-40. PMID:11884133 doi:http://dx.doi.org/10.1006/jmbi.2001.5376
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