5afo: Difference between revisions
No edit summary |
No edit summary |
||
| Line 3: | Line 3: | ||
<StructureSection load='5afo' size='340' side='right'caption='[[5afo]], [[Resolution|resolution]] 1.82Å' scene=''> | <StructureSection load='5afo' size='340' side='right'caption='[[5afo]], [[Resolution|resolution]] 1.82Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5afo]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5afo]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_LF82 Escherichia coli LF82]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AFO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5AFO FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5afo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5afo OCA], [https://pdbe.org/5afo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5afo RCSB], [https://www.ebi.ac.uk/pdbsum/5afo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5afo ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A0M3KL51_ECOLX A0A0M3KL51_ECOLX] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 23: | Line 25: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Escherichia coli | [[Category: Escherichia coli LF82]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Coppens | [[Category: Coppens F]] | ||
[[Category: Iyyathurai | [[Category: Iyyathurai J]] | ||
[[Category: Remaut | [[Category: Remaut H]] | ||
Revision as of 07:56, 25 May 2023
Long Polar Fimbriae adhesin LpfD from the adherent invasive E. coli strain LF82Long Polar Fimbriae adhesin LpfD from the adherent invasive E. coli strain LF82
Structural highlights
FunctionPublication Abstract from PubMedCrohn's disease (CD) is an inflammatory bowel disease characterized by an exaggerated immune response to commensal microbiota in the intestines of patients. Metagenomic studies have identified specific bacterial species and strains with increased prevalence in CD patients, amongst which is the adherent-invasive Escherichia coli (AIEC) strain LF82. AIEC strains express long polar fimbriae (LPF), which are known to target Peyer's patches in a mouse CD model. Here, the recombinant production of a soluble, self-complemented construct of the LpfD protein of E. coli LF82 is reported and it is demonstrated that it forms the adhesive tip subunit of LPF. The LpfD crystal reveals an N-terminal adhesin domain and a C-terminal pilin domain that connects the adhesin to the minor pilus subunit LpfE. Surface topology and sequence conservation in the adhesin domain hint at a putative receptor-binding pocket as found in the Klebsiella pneumoniae MrkD and E. coli F17-G (GafD) adhesins. Immunohistostaining of murine intestinal tissue sections revealed that LpfD specifically binds to the intestinal mucosa and submucosa. LpfD binding was found to be resistant to treatment with O- or N-glycosidases, but was lost in collagenase-treated tissue sections, indicating the possible involvement of an intestinal matrix-associated protein as the LpfD receptor. LpfD strongly adhered to isolated fibronectin in an in vitro assay, and showed lower levels of binding to collagen V and laminin and no binding to collagens I, III and IV. Structural and adhesive properties of the long polar fimbriae protein LpfD from adherent-invasive Escherichia coli.,Coppens F, Iyyathurai J, Ruer S, Fioravanti A, Taganna J, Vereecke L, De Greve H, Remaut H Acta Crystallogr D Biol Crystallogr. 2015 Aug 1;71(Pt 8):1615-26. doi:, 10.1107/S1399004715009803. Epub 2015 Jul 28. PMID:26249343[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||