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| | <StructureSection load='3gfu' size='340' side='right'caption='[[3gfu]], [[Resolution|resolution]] 1.99Å' scene=''> | | <StructureSection load='3gfu' size='340' side='right'caption='[[3gfu]], [[Resolution|resolution]] 1.99Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3gfu]] is a 4 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=3GFU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3GFU FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3gfu]] is a 4 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=3GFU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3GFU 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]] 1.991Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3gew|3gew]], [[3f65|3f65]], [[3f6l|3f6l]], [[3f6i|3f6i]], [[2j6g|2j6g]], [[2j6r|2j6r]], [[3gea|3gea]], [[3ggh|3ggh]], [[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">faeE ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895]), 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=3gfu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gfu OCA], [https://pdbe.org/3gfu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3gfu RCSB], [https://www.ebi.ac.uk/pdbsum/3gfu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3gfu 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=3gfu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gfu OCA], [https://pdbe.org/3gfu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3gfu RCSB], [https://www.ebi.ac.uk/pdbsum/3gfu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3gfu ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/FAEE_ECOLX FAEE_ECOLX]] Mediates assembly of pili by forming soluble multimeric complexes with pili subunits as an intermediate step in the assembly process. This protein is involved in K88 pili assembly. Protects pilin protein from proteolytic degradation by DegP and from premature polymerization.
| + | [https://www.uniprot.org/uniprot/Q6T3W5_ECOLX Q6T3W5_ECOLX] |
| | == 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: Chaperone]]
| + | |
| - | [[Category: Fimbrium]]
| + | |
| - | [[Category: Immunoglobulin domain]]
| + | |
| - | [[Category: Immunoglobulin like fold]]
| + | |
| Structural highlights
Function
Q6T3W5_ECOLX
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.
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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