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| | <StructureSection load='1yu3' size='340' side='right'caption='[[1yu3]], [[Resolution|resolution]] 2.52Å' scene=''> | | <StructureSection load='1yu3' size='340' side='right'caption='[[1yu3]], [[Resolution|resolution]] 2.52Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1yu3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacteriophage_bip-1 Bacteriophage bip-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YU3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YU3 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1yu3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bordetella_phage_BIP-1 Bordetella phage BIP-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YU3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YU3 FirstGlance]. <br> |
| - | </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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.52Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1yu0|1yu0]], [[1yu1|1yu1]], [[1yu2|1yu2]], [[1yu4|1yu4]]</div></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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1yu3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yu3 OCA], [https://pdbe.org/1yu3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yu3 RCSB], [https://www.ebi.ac.uk/pdbsum/1yu3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yu3 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=1yu3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yu3 OCA], [https://pdbe.org/1yu3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yu3 RCSB], [https://www.ebi.ac.uk/pdbsum/1yu3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yu3 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://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>
| + | [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> |
| | <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: Bacteriophage bip-1]] | + | [[Category: Bordetella phage BIP-1]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Ghosh, P]] | + | [[Category: Ghosh P]] |
| - | [[Category: Lawton, J A]] | + | [[Category: Lawton JA]] |
| - | [[Category: McMahon, S A]] | + | [[Category: McMahon SA]] |
| - | [[Category: Miller, J L]] | + | [[Category: Miller JL]] |
| - | [[Category: Beta prism]]
| + | |
| - | [[Category: Beta sandwich]]
| + | |
| - | [[Category: C-type lectin]]
| + | |
| - | [[Category: Diversity-generating retroelement]]
| + | |
| - | [[Category: Variability]]
| + | |
| - | [[Category: Viral protein]]
| + | |
| 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]
Publication Abstract from PubMed
Only few instances are known of protein folds that tolerate massive sequence variation for the sake of binding diversity. The most extensively characterized is the immunoglobulin fold. We now add to this the C-type lectin (CLec) fold, as found in the major tropism determinant (Mtd), a retroelement-encoded receptor-binding protein of Bordetella bacteriophage. Variation in Mtd, with its approximately 10(13) possible sequences, enables phage adaptation to Bordetella spp. Mtd is an intertwined, pyramid-shaped trimer, with variable residues organized by its CLec fold into discrete receptor-binding sites. The CLec fold provides a highly static scaffold for combinatorial display of variable residues, probably reflecting a different evolutionary solution for balancing diversity against stability from that in the immunoglobulin fold. Mtd variants are biased toward the receptor pertactin, and there is evidence that the CLec fold is used broadly for sequence variation by related retroelements.
The C-type lectin fold as an evolutionary solution for massive sequence variation.,McMahon SA, Miller JL, Lawton JA, Kerkow DE, Hodes A, Marti-Renom MA, Doulatov S, Narayanan E, Sali A, Miller JF, Ghosh P Nat Struct Mol Biol. 2005 Oct;12(10):886-92. Epub 2005 Sep 18. PMID:16170324[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
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
- ↑ McMahon SA, Miller JL, Lawton JA, Kerkow DE, Hodes A, Marti-Renom MA, Doulatov S, Narayanan E, Sali A, Miller JF, Ghosh P. The C-type lectin fold as an evolutionary solution for massive sequence variation. Nat Struct Mol Biol. 2005 Oct;12(10):886-92. Epub 2005 Sep 18. PMID:16170324 doi:nsmb992
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