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| | <StructureSection load='3ggh' size='340' side='right'caption='[[3ggh]], [[Resolution|resolution]] 1.64Å' scene=''> | | <StructureSection load='3ggh' size='340' side='right'caption='[[3ggh]], [[Resolution|resolution]] 1.64Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3ggh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GGH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3GGH FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3ggh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GGH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3GGH FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.639Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3gea|3gea]], [[3gew|3gew]], [[3gfu|3gfu]], [[2j6g|2j6g]], [[2j6r|2j6r]], [[3f65|3f65]], [[3hlr|3hlr]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">faeG ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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=3ggh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ggh OCA], [https://pdbe.org/3ggh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ggh RCSB], [https://www.ebi.ac.uk/pdbsum/3ggh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ggh 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=3ggh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ggh OCA], [https://pdbe.org/3ggh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ggh RCSB], [https://www.ebi.ac.uk/pdbsum/3ggh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ggh ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/FAEG3_ECOLX FAEG3_ECOLX]] K88 major fimbrial subunit. Fimbriae (also called pili), are polar filaments radiating from the surface of the bacterium to a length of 0.5-1.5 micrometers and numbering 100-300 per cell. They enable bacteria to colonize the epithelium of specific host organs.
| + | [https://www.uniprot.org/uniprot/FAEG3_ECOLX FAEG3_ECOLX] K88 major fimbrial subunit. Fimbriae (also called pili), are polar filaments radiating from the surface of the bacterium to a length of 0.5-1.5 micrometers and numbering 100-300 per cell. They enable bacteria to colonize the epithelium of specific host organs. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bouckaert, J]] | + | [[Category: Bouckaert J]] |
| - | [[Category: Buts, L]] | + | [[Category: Buts L]] |
| - | [[Category: Garcia-Pino, A]] | + | [[Category: De Greve H]] |
| - | [[Category: Greve, H De]]
| + | [[Category: Garcia-Pino A]] |
| - | [[Category: Molle, I Van]] | + | [[Category: Moonens K]] |
| - | [[Category: Moonens, K]] | + | [[Category: Van Molle I]] |
| - | [[Category: Cell adhesion]] | + | |
| - | [[Category: Fimbrium]]
| + | |
| - | [[Category: Immunoglobulin like fold]]
| + | |
| Structural highlights
Function
FAEG3_ECOLX K88 major fimbrial subunit. Fimbriae (also called pili), are polar filaments radiating from the surface of the bacterium to a length of 0.5-1.5 micrometers and numbering 100-300 per cell. They enable bacteria to colonize the epithelium of specific host organs.
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
Enterotoxigenic Escherichia coli expressing F4 fimbriae are the major cause of porcine colibacillosis and are responsible for significant death and morbidity in neonatal and postweaned piglets. Via the chaperone-usher pathway, F4 fimbriae are assembled into thin, flexible polymers mainly composed of the single-domain adhesin FaeG. The F4 fimbrial system has been labeled eccentric because the F4 pilins show some features distinct from the features of pilins of other chaperone-usher-assembled structures. In particular, FaeG is much larger than other pilins (27 versus approximately 17 kDa), grafting an additional carbohydrate binding domain on the common immunoglobulin-like core. Structural data of FaeG during different stages of the F4 fimbrial biogenesis process, combined with differential scanning calorimetry measurements, confirm the general principles of the donor strand complementation/exchange mechanisms taking place during pilus biogenesis via the chaperone-usher pathway.
Structural and thermodynamic characterization of pre- and postpolymerization states in the F4 fimbrial subunit FaeG.,Van Molle I, Moonens K, Garcia-Pino A, Buts L, De Kerpel M, Wyns L, Bouckaert J, De Greve H J Mol Biol. 2009 Dec 18;394(5):957-67. Epub 2009 Sep 30. PMID:19799915[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Van Molle I, Moonens K, Garcia-Pino A, Buts L, De Kerpel M, Wyns L, Bouckaert J, De Greve H. Structural and thermodynamic characterization of pre- and postpolymerization states in the F4 fimbrial subunit FaeG. J Mol Biol. 2009 Dec 18;394(5):957-67. Epub 2009 Sep 30. PMID:19799915 doi:10.1016/j.jmb.2009.09.059
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