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| | ==Major Tropism Determinant P1 (Mtd-P1) Variant Complexed with Bordetella brochiseptica Virulence Factor Pertactin extracellular domain (Prn-E).== | | ==Major Tropism Determinant P1 (Mtd-P1) Variant Complexed with Bordetella brochiseptica Virulence Factor Pertactin extracellular domain (Prn-E).== |
| - | <StructureSection load='2iou' size='340' side='right' caption='[[2iou]], [[Resolution|resolution]] 3.16Å' scene=''> | + | <StructureSection load='2iou' size='340' side='right'caption='[[2iou]], [[Resolution|resolution]] 3.16Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2iou]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Alcaligenes_bronchisepticus Alcaligenes bronchisepticus] and [http://en.wikipedia.org/wiki/Bpbpp Bpbpp]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IOU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2IOU FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2iou]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Bordetella_bronchiseptica_RB50 Bordetella bronchiseptica RB50] and [https://en.wikipedia.org/wiki/Bordetella_virus_BPP1 Bordetella virus BPP1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IOU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IOU FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 3.16Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1yu0|1yu0]], [[1dab|1dab]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Mtd ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=194699 BPBPP]), Prn ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=257310 Alcaligenes bronchisepticus])</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=2iou FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iou OCA], [https://pdbe.org/2iou PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2iou RCSB], [https://www.ebi.ac.uk/pdbsum/2iou PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2iou 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=2iou FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iou OCA], [http://pdbe.org/2iou PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2iou RCSB], [http://www.ebi.ac.uk/pdbsum/2iou PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2iou ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/Q775D6_BPBPP Q775D6_BPBPP]] Tail fiber protein located at the distal ends of the fibers that binds to the adhesion receptors on the host surface, thereby determining the host range. The phage can alter its tropism by modifying this protein. Variants are expressed through a diversity-generating retroelement (DGR) that creates mutant copies of a template repeat and replaces the end of the tail fiber receptor-binding protein with these sequences, thus changing the host range. Milliards of variants of the fiber receptor-binding protein can be created with this system.<ref>PMID:15386016</ref> [[http://www.uniprot.org/uniprot/PERT_BORBR PERT_BORBR]] Agglutinogen that binds to eukaryotic cells; a process mediated by the R-G-D sequence. Pertactin may have a role in bacterial adhesion, and thus play a role in virulence. May contribute to the disease state of whooping cough. | + | [https://www.uniprot.org/uniprot/FIBD_BPBPP FIBD_BPBPP] Tail fiber protein located at the distal ends of the fibers that binds to the adhesion receptors on the host surface, thereby determining the host range. The phage can alter its tropism by modifying this protein. Variants are expressed through a diversity-generating retroelement (DGR) that creates mutant copies of a template repeat and replaces the end of the tail fiber receptor-binding protein with these sequences, thus changing the host range. Milliards of variants of the fiber receptor-binding protein can be created with this system.<ref>PMID:15386016</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| | Check<jmol> | | Check<jmol> |
| | <jmolCheckbox> | | <jmolCheckbox> |
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/io/2iou_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/io/2iou_consurf.spt"</scriptWhenChecked> |
| | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
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| | </div> | | </div> |
| | <div class="pdbe-citations 2iou" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 2iou" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Pertussis toxin|Pertussis toxin]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Alcaligenes bronchisepticus]] | + | [[Category: Bordetella bronchiseptica RB50]] |
| - | [[Category: Bpbpp]] | + | [[Category: Bordetella virus BPP1]] |
| - | [[Category: Ghosh, P]] | + | [[Category: Large Structures]] |
| - | [[Category: Miller, J L]] | + | [[Category: Ghosh P]] |
| - | [[Category: Mtd]] | + | [[Category: Miller JL]] |
| - | [[Category: Pertactin]]
| + | |
| - | [[Category: Prn]]
| + | |
| - | [[Category: Viral protein-membrane protein complex]]
| + | |
| Structural highlights
Function
FIBD_BPBPP Tail fiber protein located at the distal ends of the fibers that binds to the adhesion receptors on the host surface, thereby determining the host range. The phage can alter its tropism by modifying this protein. Variants are expressed through a diversity-generating retroelement (DGR) that creates mutant copies of a template repeat and replaces the end of the tail fiber receptor-binding protein with these sequences, thus changing the host range. Milliards of variants of the fiber receptor-binding protein can be created with this system.[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
Diversity-generating retroelements (DGRs) recognize novel ligands through massive protein sequence variation, a property shared uniquely with the adaptive immune response. Little is known about how recognition is achieved by DGR variable proteins. Here, we present the structure of the Bordetella bacteriophage DGR variable protein major tropism determinant (Mtd) bound to the receptor pertactin, revealing remarkable adaptability in the static binding sites of Mtd. Despite large dissimilarities in ligand binding mode, principles underlying selective recognition were strikingly conserved between Mtd and immunoreceptors. Central to this was the differential amplification of binding strengths by avidity (i.e., multivalency), which not only relaxed the demand for optimal complementarity between Mtd and pertactin but also enhanced distinctions among binding events to provide selectivity. A quantitatively similar balance between complementarity and avidity was observed for Bordetella bacteriophage DGR as occurs in the immune system, suggesting that variable repertoires operate under a narrow set of conditions to recognize novel ligands.
Selective ligand recognition by a diversity-generating retroelement variable protein.,Miller JL, Le Coq J, Hodes A, Barbalat R, Miller JF, Ghosh P PLoS Biol. 2008 Jun 3;6(6):e131. PMID:18532877[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Doulatov S, Hodes A, Dai L, Mandhana N, Liu M, Deora R, Simons RW, Zimmerly S, Miller JF. Tropism switching in Bordetella bacteriophage defines a family of diversity-generating retroelements. Nature. 2004 Sep 23;431(7007):476-81. PMID:15386016 doi:http://dx.doi.org/10.1038/nature02833
- ↑ Miller JL, Le Coq J, Hodes A, Barbalat R, Miller JF, Ghosh P. Selective ligand recognition by a diversity-generating retroelement variable protein. PLoS Biol. 2008 Jun 3;6(6):e131. PMID:18532877 doi:10.1371/journal.pbio.0060131
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