3BFQ

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

3BFQ の概要

• エントリーDOI: 10.2210/pdb3bfq/pdb
• 分子名称: Protein fimG, Protein fimF, COBALT (II) ION, ... (4 entities in total)
• 機能のキーワード: incomplete ig-like fold, donor strand exchange, cell projection, fimbrium, cell adhesion, structural protein-structural protein complex, structural protein/structural protein
• 由来する生物種: Escherichia coli str. K12 substr.; 詳細
• 細胞内の位置: Fimbrium: P08190 P08189
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 15464.68

構造登録者

Eidam, O.,Capitani, G.,Grutter, M.G. (登録日: 2007-11-23, 公開日: 2008-03-04, 最終更新日: 2021-10-20)

主引用文献

Puorger, C.,Eidam, O.,Capitani, G.,Erilov, D.,Grutter, M.G.,Glockshuber, R.
Infinite Kinetic Stability against Dissociation of Supramolecular Protein Complexes through Donor Strand Complementation
Structure, 16:631-642, 2008

PubMed Abstract: 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.

PubMed: 18400183
DOI: 10.1016/j.str.2008.01.013

実験手法

X-RAY DIFFRACTION (1.34 Å)