3bfq: Difference between revisions

Revision as of 13:58, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:3bfq.png

Template:STRUCTURE 3bfq

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

Template:ABSTRACT PUBMED 18400183

About this StructureAbout this Structure

3BFQ is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

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

Page seeded by OCA on Mon Jul 28 13:58:47 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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 {{STRUCTURE_3bfq|  PDB=3bfq  |  SCENE=  }}
-'''Crystal structure of truncated FimG (FimGt) in complex with the donor strand peptide of FimF (DSF)'''
+===Crystal structure of truncated FimG (FimGt) in complex with the donor strand peptide of FimF (DSF)===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_18400183}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 18400183 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_18400183}}
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 [[Category: Incomplete ig-like fold]]
 [[Category: Structural protein/structural protein complex]]
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