5iqm: Difference between revisions
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==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_T4R-T6R-D13N== | |||
<StructureSection load='5iqm' size='340' side='right' caption='[[5iqm]], [[Resolution|resolution]] 1.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5iqm]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IQM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5IQM FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene></td></tr> | |||
<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=5iqm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5iqm OCA], [http://pdbe.org/5iqm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5iqm RCSB], [http://www.ebi.ac.uk/pdbsum/5iqm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5iqm ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[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. | |||
<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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 5iqm" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Capitani, G]] | |||
[[Category: Eras, J]] | [[Category: Eras, J]] | ||
[[Category: | [[Category: Giese, C]] | ||
[[Category: Glockshuber, R]] | |||
[[Category: Kern, A]] | [[Category: Kern, A]] | ||
[[Category: | [[Category: Scharer, M A]] | ||
[[Category: | [[Category: Cell adhesion]] | ||
[[Category: | [[Category: Complex]] | ||
[[Category: Fimgt]] | |||
[[Category: Protein]] | |||
