5dcq: Difference between revisions
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The | ==Crystal structure of bacterial adhesin, FNE from Streptococcus equi spp. equi.== | ||
<StructureSection load='5dcq' size='340' side='right'caption='[[5dcq]], [[Resolution|resolution]] 1.83Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5dcq]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_equi_subsp._equi Streptococcus equi subsp. equi] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DCQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DCQ FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.83Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</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=5dcq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dcq OCA], [https://pdbe.org/5dcq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5dcq RCSB], [https://www.ebi.ac.uk/pdbsum/5dcq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5dcq ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q93ED6_9STRE Q93ED6_9STRE] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Streptococcus equi is a horse pathogen belonging to Lancefield group C. Infection by S. equi ssp. equi causes strangles, a serious and highly contagious disease of the upper respiratory tract. S. equi ssp. equi secretes a fibronectin (Fn)-binding protein, FNE, that does not contain cell wall-anchoring motifs. FNE binds to the gelatin-binding domain (GBD) of Fn, composed of the motifs (6) FI (12) FII (789) FI . FNE lacks the canonical Fn-binding peptide repeats observed in many microbial surface components recognizing adhesive matrix molecules. We found that the interaction between FNE and the human GBD is mediated by the binding of the disordered C-terminal region (residues 208-262) of FNE to the (789) FI GBD subfragment. The crystal structure of FNE showed that it is similar to the minor pilus protein Spy0125 of Streptococcus pyogenes, found at the end of pilus polymers and responsible for adhesion. FNE and Spy0125 both have a superimposable internal thioester bond between highly conserved Cys and Gln residues. Small-angle X-ray scattering of the FNE-(789) FI complex provided a model that aligns the C-terminal peptide of FNE with the E-strands of the FI domains, adopting the beta-zipper extension model observed in previous structures of microbial surface components recognizing adhesive matrix molecule adhesion peptides bound to FI domains. | |||
Structural and functional analysis of the fibronectin-binding protein FNE from Streptococcus equi spp. equi.,Tiouajni M, Durand D, Blondeau K, Graille M, Urvoas A, Valerio-Lepiniec M, Guellouz A, Aumont-Nicaise M, Minard P, van Tilbeurgh H FEBS J. 2014 Dec;281(24):5513-31. doi: 10.1111/febs.13092. Epub 2014 Nov 4. PMID:25290767<ref>PMID:25290767</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Graille | <div class="pdbe-citations 5dcq" style="background-color:#fffaf0;"></div> | ||
[[Category: Tiouajni | == References == | ||
[[Category: Van Tilbeurgh | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Streptococcus equi subsp. equi]] | |||
[[Category: Synthetic construct]] | |||
[[Category: Graille M]] | |||
[[Category: Tiouajni M]] | |||
[[Category: Van Tilbeurgh H]] | |||
Latest revision as of 14:25, 10 January 2024
Crystal structure of bacterial adhesin, FNE from Streptococcus equi spp. equi.Crystal structure of bacterial adhesin, FNE from Streptococcus equi spp. equi.
Structural highlights
FunctionPublication Abstract from PubMedStreptococcus equi is a horse pathogen belonging to Lancefield group C. Infection by S. equi ssp. equi causes strangles, a serious and highly contagious disease of the upper respiratory tract. S. equi ssp. equi secretes a fibronectin (Fn)-binding protein, FNE, that does not contain cell wall-anchoring motifs. FNE binds to the gelatin-binding domain (GBD) of Fn, composed of the motifs (6) FI (12) FII (789) FI . FNE lacks the canonical Fn-binding peptide repeats observed in many microbial surface components recognizing adhesive matrix molecules. We found that the interaction between FNE and the human GBD is mediated by the binding of the disordered C-terminal region (residues 208-262) of FNE to the (789) FI GBD subfragment. The crystal structure of FNE showed that it is similar to the minor pilus protein Spy0125 of Streptococcus pyogenes, found at the end of pilus polymers and responsible for adhesion. FNE and Spy0125 both have a superimposable internal thioester bond between highly conserved Cys and Gln residues. Small-angle X-ray scattering of the FNE-(789) FI complex provided a model that aligns the C-terminal peptide of FNE with the E-strands of the FI domains, adopting the beta-zipper extension model observed in previous structures of microbial surface components recognizing adhesive matrix molecule adhesion peptides bound to FI domains. Structural and functional analysis of the fibronectin-binding protein FNE from Streptococcus equi spp. equi.,Tiouajni M, Durand D, Blondeau K, Graille M, Urvoas A, Valerio-Lepiniec M, Guellouz A, Aumont-Nicaise M, Minard P, van Tilbeurgh H FEBS J. 2014 Dec;281(24):5513-31. doi: 10.1111/febs.13092. Epub 2014 Nov 4. PMID:25290767[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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