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| | <StructureSection load='3bfw' size='340' side='right'caption='[[3bfw]], [[Resolution|resolution]] 1.80Å' scene=''> | | <StructureSection load='3bfw' size='340' side='right'caption='[[3bfw]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3bfw]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecow3 Ecow3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BFW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BFW FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3bfw]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [https://en.wikipedia.org/wiki/Escherichia_coli_str._K-12_substr._W3110 Escherichia coli str. K-12 substr. W3110]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BFW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BFW FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=YT3:YTTRIUM+(III)+ION'>YT3</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]] 1.8Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3bfq|3bfq]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=YT3:YTTRIUM+(III)+ION'>YT3</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fimG ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=316407 ECOW3])</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=3bfw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bfw OCA], [https://pdbe.org/3bfw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bfw RCSB], [https://www.ebi.ac.uk/pdbsum/3bfw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bfw 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=3bfw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bfw OCA], [https://pdbe.org/3bfw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bfw RCSB], [https://www.ebi.ac.uk/pdbsum/3bfw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bfw ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/FIMG_ECOLI FIMG_ECOLI]] Involved in regulation of length and mediation of adhesion of type 1 fimbriae (but not necessary for the production of fimbriae). Involved in the integration of FimH in the fimbriae. [[https://www.uniprot.org/uniprot/FIMF_ECOLI FIMF_ECOLI]] Involved in regulation of length and mediation of adhesion of type 1 fimbriae (but not necessary for the production of fimbriae). Involved in the integration of FimH in the fimbriae.
| + | [https://www.uniprot.org/uniprot/FIMG_ECOLI FIMG_ECOLI] Involved in regulation of length and mediation of adhesion of type 1 fimbriae (but not necessary for the production of fimbriae). Involved in the integration of FimH in the fimbriae. |
| | == 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: Ecow3]] | + | [[Category: Escherichia coli]] |
| | + | [[Category: Escherichia coli str. K-12 substr. W3110]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Capitani, G]] | + | [[Category: Capitani G]] |
| - | [[Category: Eidam, O]] | + | [[Category: Eidam O]] |
| - | [[Category: Grutter, M G]] | + | [[Category: Grutter MG]] |
| - | [[Category: Cell adhesion]]
| + | |
| - | [[Category: Cell projection]]
| + | |
| - | [[Category: Donor strand exchange]]
| + | |
| - | [[Category: Fimbrium]]
| + | |
| - | [[Category: Incomplete ig-like fold]]
| + | |
| - | [[Category: Structural protein-structural protein complex]]
| + | |
| Structural highlights
Function
FIMG_ECOLI Involved in regulation of length and mediation of adhesion of type 1 fimbriae (but not necessary for the production of fimbriae). Involved in the integration of FimH in the fimbriae.
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
Adhesive type 1 pili from uropathogenic Escherichia coli strains are heat and denaturant resistant, filamentous protein complexes. Individual pilus subunits associate through "donor strand complementation," whereby the incomplete immunoglobulin-like fold of each subunit is completed by the N-terminal extension of a neighboring subunit. We show that antiparallel donor strand insertion generally causes nonequilibrium behavior in protein folding and extreme activation energy barriers for dissociation of subunit-subunit complexes. We identify the most kinetically stable, noncovalent protein complex known to date. The complex between the pilus subunit FimG and the donor strand peptide of the subunit FimF shows an extrapolated dissociation half-life of 3 x 10(9) years. The 15 residue peptide forms ideal intermolecular beta sheet H-bonds with FimG over 10 residues, and its hydrophobic side chains strongly interact with the hydrophobic core of FimG. The results show that kinetic stability and nonequilibrium behavior in protein folding confers infinite stability against dissociation in extracellular protein complexes.
Infinite kinetic stability against dissociation of supramolecular protein complexes through donor strand complementation.,Puorger C, Eidam O, Capitani G, Erilov D, Grutter MG, Glockshuber R Structure. 2008 Apr;16(4):631-42. PMID:18400183[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Puorger C, Eidam O, Capitani G, Erilov D, Grutter MG, Glockshuber R. Infinite kinetic stability against dissociation of supramolecular protein complexes through donor strand complementation. Structure. 2008 Apr;16(4):631-42. PMID:18400183 doi:10.1016/j.str.2008.01.013
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