2JMR

NMR structure of the E. coli type 1 pilus subunit FimF

2JMR の概要

• エントリーDOI: 10.2210/pdb2jmr/pdb
• NMR情報: BMRB: 15032
• 分子名称: fimF (1 entity in total)
• 機能のキーワード: protein, cell adhesion
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 19188.38

構造登録者

Gossert, A.D.,Bettendorff, P.,Puorger, C.,Vetsch, M.,Herrmann, T.,Fiorito, F.,Hiller, S.,Glockshuber, R.,Wuthrich, K. (登録日: 2006-11-29, 公開日: 2007-10-30, 最終更新日: 2024-11-06)

主引用文献

Gossert, A.D.,Bettendorff, P.,Puorger, C.,Vetsch, M.,Herrmann, T.,Glockshuber, R.,Wuthrich, K.
NMR structure of the Escherichia coli type 1 pilus subunit FimF and its interactions with other pilus subunits.
J.Mol.Biol., 375:752-763, 2008

PubMed Abstract: Type 1 pili from uropathogenic Escherichia coli strains mediate bacterial attachment to target receptors on the host tissue. They are composed of up to 3000 copies of the subunit FimA, which form the stiff, helical pilus rod, and the subunits FimF, FimG, and FimH, which form the linear tip fibrillum. All subunits in the pilus interact via donor strand complementation, in which the incomplete immunoglobulin-like fold of each subunit is complemented by insertion of an N-terminal extension from the following subunit. We determined the NMR structure of a monomeric, self-complemented variant of FimF, FimF(F), which has a second FimF donor strand segment fused to its C-terminus that enables intramolecular complementation of the FimF fold. NMR studies on bimolecular complexes between FimF(F) and donor strand-depleted variants of FimF and FimG revealed that the relative orientations of neighboring domains in the tip fibrillum cover a wide range. The data provide strong support for the intrinsic flexibility of the tip fibrillum. They lend further support to the hypothesis that this flexibility would significantly increase the probability that the adhesin at the distal end of the fibrillum successfully targets host cell receptors.

PubMed: 18048056
DOI: 10.1016/j.jmb.2007.10.059

実験手法

SOLUTION NMR