2LW1

The C-terminal domain of the Uup protein is a DNA-binding coiled coil motif

2LW1 の概要

• エントリーDOI: 10.2210/pdb2lw1/pdb
• NMR情報: BMRB: 17989
• 分子名称: ABC transporter ATP-binding protein uup (1 entity in total)
• 機能のキーワード: abc reg subfamily, dna binding protein
• 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: 12164.54

構造登録者

Carlier, L.,Haase, A.S.,Burgos Zepeda, M.Y.,Dassa, E.,Lequin, O. (登録日: 2012-07-19, 公開日: 2012-09-19, 最終更新日: 2024-05-15)

主引用文献

Carlier, L.,Haase, A.S.,Burgos Zepeda, M.Y.,Dassa, E.,Lequin, O.
The C-terminal domain of the Uup protein is a DNA-binding coiled coil motif.
J.Struct.Biol., 180:577-584, 2012

PubMed Abstract: The bacterial Uup protein belongs to the REG subfamily of soluble ATP-binding cassette (ABC) ATPases, and is implicated in precise excision of transposons. In Escherichia coli, the uup gene encodes a 72 kDa polypeptide that comprises two ABC domains, separated by a linker region, and a 12kDa C-terminal domain (CTD). Uup binds double-stranded DNA with no sequence specificity, and we previously demonstrated that the CTD domain is a crucial region that participates in DNA-binding activity. We report herein the NMR structure of Uup CTD, consisting of an intramolecular antiparallel two-stranded coiled coil motif. Structural comparison with analogous coiled coil domains reveals that Uup CTD contains an atypical 3(10)-helix in the α-hairpin region that contributes to the hydrophobic core. Using NMR titration experiments, we identified residues of the CTD domain involved in the binding to double-stranded DNA. These residues are located on two opposite surfaces at the base of the coiled coil, formed by the N- and C-terminal extremities, where a strictly conserved proline residue induces an overwinding of the coiled coil. Finally, preliminary analysis of NMR spectra recorded on distinct Uup constructs precludes a fully flexible positioning of the CTD domain in full-length Uup. These structural data are the first reported for a non-ATPase domain within ABC REG subfamily.

PubMed: 22995754
DOI: 10.1016/j.jsb.2012.09.005

実験手法

SOLUTION NMR