View source for 5iqn


==Crystal structure of the E. coli type 1 pilus subunit FimG (engineered variant with substitution Q134E; N-terminal FimG residues 1-12 truncated) in complex with the donor strand peptide DsF_SRIRIRGYVR==
<StructureSection load='5iqn' size='340' side='right'caption='[[5iqn]], [[Resolution|resolution]] 1.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5iqn]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IQN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5IQN FirstGlance]. <br>
</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&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></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=5iqn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5iqn OCA], [https://pdbe.org/5iqn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5iqn RCSB], [https://www.ebi.ac.uk/pdbsum/5iqn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5iqn ProSAT]</span></td></tr>
</table>
== 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.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The complex between the bacterial type 1 pilus subunit FimG and the peptide corresponding to the N-terminal extension (termed donor strand, Ds) of the partner subunit FimF (DsF) shows the strongest reported noncovalent molecular interaction, with a dissociation constant (KD ) of 1.5x10-20 m. However, the complex only exhibits a slow association rate of 330 m-1 s-1 that limits technical applications, such as its use in affinity purification. Herein, a structure-based approach was used to design pairs of FimGt (a FimG variant lacking its own N-terminal extension) and DsF variants with enhanced electrostatic surface complementarity. Association of the best mutant FimGt/DsF pairs was accelerated by more than two orders of magnitude, while the dissociation rates and 3D structures of the improved complexes remained essentially unperturbed. A KD value of 8.8x10-22 m was obtained for the best mutant complex, which is the lowest value reported to date for a protein/ligand complex.

Accelerating the Association of the Most Stable Protein-Ligand Complex by more than Two Orders of Magnitude.,Giese C, Eras J, Kern A, Scharer MA, Capitani G, Glockshuber R Angew Chem Int Ed Engl. 2016 Jun 28. doi: 10.1002/anie.201603652. PMID:27351462<ref>PMID:27351462</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5iqn" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Capitani G]]
[[Category: Eras J]]
[[Category: Giese C]]
[[Category: Glockshuber R]]
[[Category: Kern A]]
[[Category: Scharer MA]]