5iqm

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m (Protected "5iqm" [edit=sysop:move=sysop])
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'''Unreleased structure'''
 
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The entry 5iqm is ON HOLD until Paper Publication
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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==
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<StructureSection load='5iqm' size='340' side='right' caption='[[5iqm]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
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== Structural highlights ==
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<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>
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</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>
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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=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>
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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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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Authors: Giese, C., Eras, J., Kern, A., Scharer, M.A., Capitani, G., Glockshuber, R.
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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>
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Description: 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
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 5iqm" 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>
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[[Category: Capitani, G]]
[[Category: Eras, J]]
[[Category: Eras, J]]
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[[Category: Scharer, M.A]]
 
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[[Category: Kern, A]]
 
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[[Category: Glockshuber, R]]
 
[[Category: Giese, C]]
[[Category: Giese, C]]
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[[Category: Capitani, G]]
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[[Category: Glockshuber, R]]
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[[Category: Kern, A]]
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[[Category: Scharer, M A]]
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[[Category: Cell adhesion]]
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[[Category: Complex]]
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[[Category: Fimgt]]
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[[Category: Protein]]

Revision as of 02:16, 13 July 2016

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

5iqm, resolution 1.50Å

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