2HTJ

NMR structure of E.coli PapI

2HTJ の概要

• エントリーDOI: 10.2210/pdb2htj/pdb
• 分子名称: P fimbrial regulatory protein KS71A (1 entity in total)
• 機能のキーワード: winged helix-turn-helix, pap pili, transcription activator
• 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: 9338.63

構造登録者

Kawamura, T.,Zhou, H.,Le, L.U.K.,Dahlquist, F.W. (登録日: 2006-07-25, 公開日: 2007-01-30, 最終更新日: 2024-05-29)

主引用文献

Kawamura, T.,Le, L.U.,Zhou, H.,Dahlquist, F.W.
Solution Structure of Escherichia coli PapI, a Key Regulator of the Pap Pili Phase Variation.
J.Mol.Biol., 365:1130-1142, 2007

PubMed Abstract: Pyelonephritis-associated pili (pap) allow uropathogenic Escherichia coli to bind to epithelial cells and play an important role in urinary tract infection. Expression of pap is controlled by a phase-variation mechanism, based on the two distinct heritable states that are the result of adenine N6-methylation in either of the two GATC sequences in its regulatory region. The methylation status of these two sequences is sensed by the action of two proteins, Lrp and PapI, and they play a central role in determining pap gene expression in both phase-ON and phase-OFF cells. We used modern NMR techniques to determine the solution structure and backbone dynamics of PapI. We found its overall fold resembles closely that of the winged helix-turn-helix family of DNA-binding proteins. We determined that PapI possesses its own DNA-binding activity, albeit non-sequence-specific, independent of Lrp. PapI appears to bind to DNA with a K(d) in the 10 microM range. Possible mechanisms by which PapI might participate in the regulation of the pap operon are discussed in light of these new findings.

PubMed: 17109885
DOI: 10.1016/j.jmb.2006.10.066

実験手法

SOLUTION NMR