|
|
| Line 3: |
Line 3: |
| | <StructureSection load='5jgv' size='340' side='right'caption='[[5jgv]], [[Resolution|resolution]] 1.73Å' scene=''> | | <StructureSection load='5jgv' size='340' side='right'caption='[[5jgv]], [[Resolution|resolution]] 1.73Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5jgv]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_t4_sensu_lato Enterobacteria phage t4 sensu lato]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JGV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JGV FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5jgv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_phage_T4 Escherichia phage T4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JGV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5JGV FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=HEZ:HEXANE-1,6-DIOL'>HEZ</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=V1A:S-(1-OXYL-2,2,5,5-TETRAMETHYL-2,5-DIHYDRO-1H-IMIDAZOL-4-YL)+METHANESULFONOTHIOATE'>V1A</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]] 1.732Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5jgn|5jgn]], [[5jgr|5jgr]], [[5jgu|5jgu]], [[5jgx|5jgx]], [[5jgz|5jgz]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=HEZ:HEXANE-1,6-DIOL'>HEZ</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=V1A:S-(1-OXYL-2,2,5,5-TETRAMETHYL-2,5-DIHYDRO-1H-IMIDAZOL-4-YL)+METHANESULFONOTHIOATE'>V1A</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=5jgv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jgv OCA], [https://pdbe.org/5jgv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5jgv RCSB], [https://www.ebi.ac.uk/pdbsum/5jgv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5jgv 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=5jgv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jgv OCA], [http://pdbe.org/5jgv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jgv RCSB], [http://www.ebi.ac.uk/pdbsum/5jgv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jgv ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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> | + | [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 == |
| Line 20: |
Line 19: |
| | </div> | | </div> |
| | <div class="pdbe-citations 5jgv" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 5jgv" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Lysin 3D structures|Lysin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Enterobacteria phage t4 sensu lato]] | + | [[Category: Escherichia phage T4]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lysozyme]]
| + | [[Category: Balo AR]] |
| - | [[Category: Balo, A R]] | + | [[Category: Ernst OP]] |
| - | [[Category: Ernst, O P]] | + | [[Category: Feyrer H]] |
| - | [[Category: Feyrer, H]] | + | |
| - | [[Category: Deer]]
| + | |
| - | [[Category: Epr]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Spin label]]
| + | |
| 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]
Publication Abstract from PubMed
Pulsed electron paramagnetic resonance experiments can measure individual distances between two spin-labeled side chains in proteins in the range of approximately 1.5-8 nm. However, the flexibility of traditional spin-labeled side chains leads to diffuse spin density loci and thus distance distributions with relatively broad peaks, thereby complicating the interpretation of protein conformational states. Here we analyzed the spin-labeled V1 side chain, which is internally anchored and hence less flexible. Crystal structures of V1-labeled T4 lysozyme constructs carrying the V1 side chain on alpha-helical segments suggest that V1 side chains adopt only a few discrete rotamers. In most cases, only one rotamer is observed at a given site, explaining the frequently observed narrow distance distribution for doubly V1-labeled proteins. We used the present data to derive guidelines that may allow distance interpretation of other V1-labeled proteins for higher-precision structural modeling.
Toward Precise Interpretation of DEER-Based Distance Distributions: Insights from Structural Characterization of V1 Spin-Labeled Side Chains.,Balo AR, Feyrer H, Ernst OP Biochemistry. 2016 Sep 20;55(37):5256-63. doi: 10.1021/acs.biochem.6b00608. Epub , 2016 Sep 2. PMID:27532325[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
- ↑ Balo AR, Feyrer H, Ernst OP. Toward Precise Interpretation of DEER-Based Distance Distributions: Insights from Structural Characterization of V1 Spin-Labeled Side Chains. Biochemistry. 2016 Sep 20;55(37):5256-63. doi: 10.1021/acs.biochem.6b00608. Epub , 2016 Sep 2. PMID:27532325 doi:http://dx.doi.org/10.1021/acs.biochem.6b00608
|
