3bfw

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[[Image:3bfw.jpg|left|200px]]
 
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==Crystal structure of truncated FimG (FimGt) in complex with the donor strand peptide of FimF (DSF)==
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The line below this paragraph, containing "STRUCTURE_3bfw", creates the "Structure Box" on the page.
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<StructureSection load='3bfw' size='340' side='right'caption='[[3bfw]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<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>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
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<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>
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{{STRUCTURE_3bfw| PDB=3bfw | SCENE= }}
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<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>
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</table>
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'''Crystal structure of truncated FimG (FimGt) in complex with the donor strand peptide of FimF (DSF)'''
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== Function ==
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[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.
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== Evolutionary Conservation ==
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==Overview==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bf/3bfw_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3bfw ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== 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.
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.
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==About this Structure==
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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<ref>PMID:18400183</ref>
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3BFW is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BFW OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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:[http://www.ncbi.nlm.nih.gov/pubmed/18400183 18400183]
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</div>
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<div class="pdbe-citations 3bfw" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Protein complex]]
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[[Category: Escherichia coli str. K-12 substr. W3110]]
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[[Category: Capitani, G.]]
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[[Category: Large Structures]]
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[[Category: Eidam, O.]]
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[[Category: Capitani G]]
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[[Category: Grutter, M G.]]
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[[Category: Eidam O]]
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[[Category: Cell adhesion]]
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[[Category: Grutter MG]]
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[[Category: Cell projection]]
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[[Category: Donor strand exchange]]
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[[Category: Fimbrium]]
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[[Category: Incomplete ig-like fold]]
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[[Category: Structural protein/structural protein complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Apr 24 09:32:54 2008''
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Current revision

Crystal structure of truncated FimG (FimGt) in complex with the donor strand peptide of FimF (DSF)

PDB ID 3bfw

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