3bfw

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[[Image:3bfw.png|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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<StructureSection load='3bfw' size='340' side='right' caption='[[3bfw]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3bfw]] is a 4 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3BFW FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=YT3:YTTRIUM+(III)+ION'>YT3</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3bfq|3bfq]]</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fimG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=316407 Escherichia coli str. K-12 substr. W3110])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3bfw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bfw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3bfw RCSB], [http://www.ebi.ac.uk/pdbsum/3bfw PDBsum]</span></td></tr>
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</table>
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== Function ==
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[[http://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. [[http://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.
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== Evolutionary Conservation ==
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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/initialview01.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/chain_selection.php?pdb_ID=2ata 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 ==
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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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{{STRUCTURE_3bfw| PDB=3bfw | SCENE= }}
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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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===Crystal structure of truncated FimG (FimGt) in complex with the donor strand peptide of FimF (DSF)===
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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{{ABSTRACT_PUBMED_18400183}}
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== References ==
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<references/>
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==About this Structure==
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__TOC__
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[[3bfw]] is a 4 chain structure with sequence from [http://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].
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</StructureSection>
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==Reference==
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<ref group="xtra">PMID:018400183</ref><references group="xtra"/>
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[[Category: Escherichia coli str. k-12 substr. w3110]]
[[Category: Escherichia coli str. k-12 substr. w3110]]
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[[Category: Capitani, G.]]
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[[Category: Capitani, G]]
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[[Category: Eidam, O.]]
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[[Category: Eidam, O]]
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[[Category: Grutter, M G.]]
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[[Category: Grutter, M G]]
[[Category: Cell adhesion]]
[[Category: Cell adhesion]]
[[Category: Cell projection]]
[[Category: Cell projection]]

Revision as of 20:21, 25 December 2014

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

3bfw, resolution 1.80Å

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