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| | <StructureSection load='3qr8' size='340' side='right'caption='[[3qr8]], [[Resolution|resolution]] 2.03Å' scene=''> | | <StructureSection load='3qr8' size='340' side='right'caption='[[3qr8]], [[Resolution|resolution]] 2.03Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3qr8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bpp2 Bpp2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QR8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QR8 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3qr8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_P2 Escherichia virus P2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QR8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QR8 FirstGlance]. <br> |
| - | </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=GOL:GLYCEROL'>GOL</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]] 2.03Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3qr7|3qr7]]</div></td></tr>
| + | |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">V ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10679 BPP2])</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=3qr8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qr8 OCA], [https://pdbe.org/3qr8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qr8 RCSB], [https://www.ebi.ac.uk/pdbsum/3qr8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qr8 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=3qr8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qr8 OCA], [https://pdbe.org/3qr8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qr8 RCSB], [https://www.ebi.ac.uk/pdbsum/3qr8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qr8 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/VPV_BPP2 VPV_BPP2]] Forms the small spike at the tip of the tail.
| + | [https://www.uniprot.org/uniprot/SPIKE_BPP2 SPIKE_BPP2] Forms the small spikes on the baseplate that plug the end of the tube before DNA ejection and form a channel perforating the host membrane during ejection. Involved in baseplate assembly.<ref>PMID:21821878</ref> <ref>PMID:22325780</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: Bpp2]] | + | [[Category: Escherichia virus P2]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Browning, C]] | + | [[Category: Browning C]] |
| - | [[Category: Leiman, P G]] | + | [[Category: Leiman PG]] |
| - | [[Category: Shneider, M]] | + | [[Category: Shneider M]] |
| - | [[Category: Beta-helix]]
| + | |
| - | [[Category: Cell membrane piercing]]
| + | |
| - | [[Category: Iron-binding]]
| + | |
| - | [[Category: Ob-fold]]
| + | |
| - | [[Category: Phage baseplate]]
| + | |
| - | [[Category: Tail spike]]
| + | |
| - | [[Category: Viral protein]]
| + | |
| Structural highlights
Function
SPIKE_BPP2 Forms the small spikes on the baseplate that plug the end of the tube before DNA ejection and form a channel perforating the host membrane during ejection. Involved in baseplate assembly.[1] [2]
Publication Abstract from PubMed
Bacteriophages with contractile tails and the bacterial type VI secretion system have been proposed to use a special protein to create an opening in the host cell membrane during infection. These proteins have a modular architecture but invariably contain an oligonucleotide/oligosaccharide-binding (OB-fold) domain and a long beta-helical C-terminal domain, which initiates the contact with the host cell membrane. Using X-ray crystallography and electron microscopy, we report the atomic structure of the membrane-piercing proteins from bacteriophages P2 and varphi92 and identify the residues that constitute the membrane-attacking apex. Both proteins form compact spikes with a approximately 10A diameter tip that is stabilized by a centrally positioned iron ion bound by six histidine residues. The accumulated data strongly suggest that, in the process of membrane penetration, the spikes are translocated through the lipid bilayer without undergoing major unfolding.
Phage pierces the host cell membrane with the iron-loaded spike.,Browning C, Shneider MM, Bowman VD, Schwarzer D, Leiman PG Structure. 2012 Feb 8;20(2):326-39. PMID:22325780[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Yamashita E, Nakagawa A, Takahashi J, Tsunoda K, Yamada S, Takeda S. The host-binding domain of the P2 phage tail spike reveals a trimeric iron-binding structure. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Aug 1;67(Pt 8):837-41., Epub 2011 Jul 13. PMID:21821878 doi:10.1107/S1744309111005999
- ↑ Browning C, Shneider MM, Bowman VD, Schwarzer D, Leiman PG. Phage pierces the host cell membrane with the iron-loaded spike. Structure. 2012 Feb 8;20(2):326-39. PMID:22325780 doi:10.1016/j.str.2011.12.009
- ↑ Browning C, Shneider MM, Bowman VD, Schwarzer D, Leiman PG. Phage pierces the host cell membrane with the iron-loaded spike. Structure. 2012 Feb 8;20(2):326-39. PMID:22325780 doi:10.1016/j.str.2011.12.009
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