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| | ==Structure of Phage P22 Tail Needle gp26== | | ==Structure of Phage P22 Tail Needle gp26== |
| - | <StructureSection load='2poh' size='340' side='right' caption='[[2poh]], [[Resolution|resolution]] 2.10Å' scene=''> | + | <StructureSection load='2poh' size='340' side='right'caption='[[2poh]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2poh]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacteriophage_p22-pbi Bacteriophage p22-pbi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2POH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2POH FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2poh]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_phage_P22-pbi Salmonella phage P22-pbi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2POH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2POH FirstGlance]. <br> |
| - | </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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1lkt|1lkt]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">26 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=200913 Bacteriophage P22-pbi])</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=2poh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2poh OCA], [https://pdbe.org/2poh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2poh RCSB], [https://www.ebi.ac.uk/pdbsum/2poh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2poh 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=2poh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2poh OCA], [http://pdbe.org/2poh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2poh RCSB], [http://www.ebi.ac.uk/pdbsum/2poh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2poh ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/NEEDL_BPP22 NEEDL_BPP22]] Cell-perforating component and plug protein of the phage tail machine. Host cell membrane perforation allows viral DNA ejection. Together with gp4 and gp10, gp26 is required for stabilization of the condensed DNA within the capsid by plugging the hole through which the DNA enters.<ref>PMID:18059287</ref> <ref>PMID:20817910</ref> | + | [https://www.uniprot.org/uniprot/NEEDL_BPP22 NEEDL_BPP22] Cell-perforating component and plug protein of the phage tail machine. Host cell membrane perforation allows viral DNA ejection. Together with gp4 and gp10, gp26 is required for stabilization of the condensed DNA within the capsid by plugging the hole through which the DNA enters.<ref>PMID:18059287</ref> <ref>PMID:20817910</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | <jmolCheckbox> | | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/po/2poh_consurf.spt"</scriptWhenChecked> | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/po/2poh_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacteriophage p22-pbi]] | + | [[Category: Large Structures]] |
| - | [[Category: Cingolani, G]] | + | [[Category: Salmonella phage P22-pbi]] |
| - | [[Category: Olia, A S]]
| + | [[Category: Cingolani G]] |
| - | [[Category: Fiber]]
| + | [[Category: Olia AS]] |
| - | [[Category: Heptad]]
| + | |
| - | [[Category: Membrane-penetration]]
| + | |
| - | [[Category: Trimeric coiled-coil]] | + | |
| - | [[Category: Triple beta-helix]] | + | |
| - | [[Category: Viral protein]]
| + | |
| Structural highlights
Function
NEEDL_BPP22 Cell-perforating component and plug protein of the phage tail machine. Host cell membrane perforation allows viral DNA ejection. Together with gp4 and gp10, gp26 is required for stabilization of the condensed DNA within the capsid by plugging the hole through which the DNA enters.[1] [2]
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
Bacteriophage P22 infects Salmonella enterica by injecting its genetic material through the cell envelope. During infection, a specialized tail needle, gp26, is injected into the host, likely piercing a hole in the host cell envelope. The 2.1-A crystal structure of gp26 reveals a 240-A elongated protein fiber formed by two trimeric coiled-coil domains interrupted by a triple beta-helix. The N terminus of gp26 plugs the portal protein channel, retaining the genetic material inside the virion. The C-terminal tip of the fiber exposes beta-hairpins with hydrophobic tips similar to those seen in class II fusion peptides. The alpha-helical core connecting these two functionally polarized tips presents four trimerization octads with consensus sequence IXXLXXXV. The slender conformation of the gp26 fiber minimizes the surface exposed to solvent, which is consistent with the idea that gp26 traverses the cell envelope lipid bilayers.
Structure of phage P22 cell envelope-penetrating needle.,Olia AS, Casjens S, Cingolani G Nat Struct Mol Biol. 2007 Dec 2. PMID:18059287[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Olia AS, Casjens S, Cingolani G. Structure of phage P22 cell envelope-penetrating needle. Nat Struct Mol Biol. 2007 Dec 2. PMID:18059287 doi:10.1038/nsmb1317
- ↑ Andres D, Hanke C, Baxa U, Seul A, Barbirz S, Seckler R. Tailspike interactions with lipopolysaccharide effect DNA ejection from phage P22 particles in vitro. J Biol Chem. 2010 Nov 19;285(47):36768-75. doi: 10.1074/jbc.M110.169003. Epub, 2010 Sep 3. PMID:20817910 doi:http://dx.doi.org/10.1074/jbc.M110.169003
- ↑ Olia AS, Casjens S, Cingolani G. Structure of phage P22 cell envelope-penetrating needle. Nat Struct Mol Biol. 2007 Dec 2. PMID:18059287 doi:10.1038/nsmb1317
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