|
|
| Line 3: |
Line 3: |
| | <StructureSection load='5ewx' size='340' side='right'caption='[[5ewx]], [[Resolution|resolution]] 2.60Å' scene=''> | | <StructureSection load='5ewx' size='340' side='right'caption='[[5ewx]], [[Resolution|resolution]] 2.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5ewx]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"micrococcus_aureus"_(rosenbach_1884)_zopf_1885 "micrococcus aureus" (rosenbach 1884) zopf 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EWX OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5EWX FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5ewx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_T4 Escherichia virus T4] and [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EWX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5EWX FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EYC:2,2-ETHYNE-1,2-DIYLBIS{5-[(CHLOROACETYL)AMINO]BENZENESULFONIC+ACID}'>EYC</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]] 2.6Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">spa ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 "Micrococcus aureus" (Rosenbach 1884) Zopf 1885])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EYC:2,2-ETHYNE-1,2-DIYLBIS{5-[(CHLOROACETYL)AMINO]BENZENESULFONIC+ACID}'>EYC</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=5ewx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ewx OCA], [https://pdbe.org/5ewx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ewx RCSB], [https://www.ebi.ac.uk/pdbsum/5ewx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ewx ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5ewx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ewx OCA], [http://pdbe.org/5ewx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ewx RCSB], [http://www.ebi.ac.uk/pdbsum/5ewx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ewx 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/SPA_STAAU SPA_STAAU] [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 24: |
Line 23: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Escherichia virus T4]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lysozyme]] | + | [[Category: Staphylococcus aureus]] |
| - | [[Category: Jeong, W H]] | + | [[Category: Jeong WH]] |
| - | [[Category: Lee, H]] | + | [[Category: Lee H]] |
| - | [[Category: Lee, J O]] | + | [[Category: Lee JO]] |
| - | [[Category: Song, D H]] | + | [[Category: Song DH]] |
| - | [[Category: Alpha helix]]
| + | |
| - | [[Category: Cross-linker]]
| + | |
| - | [[Category: Ey-cb]]
| + | |
| - | [[Category: Fusion]]
| + | |
| - | [[Category: Protein binding]]
| + | |
| Structural highlights
Function
SPA_STAAU 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
Building a sophisticated protein nano-assembly requires a method for linking protein components in a predictable and stable structure. Most of the cross linkers available have flexible spacers. Because of this, the linked hybrids have significant structural flexibility and the relative structure between their two components is largely unpredictable. Here we describe a method of connecting two proteins via a 'fusion alpha helix' formed by joining two pre-existing helices into a single extended helix. Because simple ligation of two helices does not guarantee the formation of a continuous helix, we used EY-CBS, a synthetic cross linker that has been shown to react selectively with cysteines in alpha-helices, to stabilize the connecting helix. Formation and stabilization of the fusion helix was confirmed by determining the crystal structures of the fusion proteins with and without bound EY-CBS. Our method should be widely applicable for linking protein building blocks to generate predictable structures.
Connecting two proteins using a fusion alpha helix stabilized by a chemical cross linker.,Jeong WH, Lee H, Song DH, Eom JH, Kim SC, Lee HS, Lee H, Lee JO Nat Commun. 2016 Mar 16;7:11031. doi: 10.1038/ncomms11031. PMID:26980593[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
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
- ↑ Jeong WH, Lee H, Song DH, Eom JH, Kim SC, Lee HS, Lee H, Lee JO. Connecting two proteins using a fusion alpha helix stabilized by a chemical cross linker. Nat Commun. 2016 Mar 16;7:11031. doi: 10.1038/ncomms11031. PMID:26980593 doi:http://dx.doi.org/10.1038/ncomms11031
|
