1yu3

From Proteopedia

(Difference between revisions)

Revision as of 16:32, 3 November 2021

Major Tropism Determinant I1 Variant

Structural highlights

1yu3 is a 1 chain structure with sequence from Bacteriophage bip-1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1yu0, 1yu1, 1yu2, 1yu4
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.^[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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1yu3"

@@ Line 3: / Line 3: @@
 <StructureSection load='1yu3' size='340' side='right'caption='[[1yu3]], [[Resolution|resolution]] 2.52&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1yu3]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/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/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>
-</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='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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1yu0|1yu0]], [[1yu1|1yu1]], [[1yu2|1yu2]], [[1yu4|1yu4]]</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='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=1yu3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yu3 OCA], [http://pdbe.org/1yu3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1yu3 RCSB], [http://www.ebi.ac.uk/pdbsum/1yu3 PDBsum], [http://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>
 == 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>
+[[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>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

1yu3

From Proteopedia

Revision as of 16:32, 3 November 2021

Major Tropism Determinant I1 Variant

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox