4MUO

The TrpD2 enzyme from E.coli: YbiB

4MUO の概要

• エントリーDOI: 10.2210/pdb4muo/pdb
• 関連するPDBエントリー: 1O17
• 分子名称: Uncharacterized protein YbiB (2 entities in total)
• 機能のキーワード: prt class iii fold, intracellular, dna binding protein
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 72331.34

構造登録者

Stutz, C.,Mayans, O. (登録日: 2013-09-23, 公開日: 2015-03-25, 最終更新日: 2024-02-28)

主引用文献

Schneider, D.,Kaiser, W.,Stutz, C.,Holinski, A.,Mayans, O.,Babinger, P.
YbiB from Escherichia coli, the Defining Member of the Novel TrpD2 Family of Prokaryotic DNA-binding Proteins.
J.Biol.Chem., 290:19527-19539, 2015

PubMed Abstract: We present the crystal structure and biochemical characterization of Escherichia coli YbiB, a member of the hitherto uncharacterized TrpD2 protein family. Our results demonstrate that the functional diversity of proteins with a common fold can be far greater than predictable by computational annotation. The TrpD2 proteins show high structural homology to anthranilate phosphoribosyltransferase (TrpD) and nucleoside phosphorylase class II enzymes but bind with high affinity (KD = 10-100 nM) to nucleic acids without detectable sequence specificity. The difference in affinity between single- and double-stranded DNA is minor. Results suggest that multiple YbiB molecules bind to one longer DNA molecule in a cooperative manner. The YbiB protein is a homodimer that, therefore, has two electropositive DNA binding grooves. But due to negative cooperativity within the dimer, only one groove binds DNA in in vitro experiments. A monomerized variant remains able to bind DNA with similar affinity, but the negative cooperative effect is eliminated. The ybiB gene forms an operon with the DNA helicase gene dinG and is under LexA control, being induced by DNA-damaging agents. Thus, speculatively, the TrpD2 proteins may be part of the LexA-controlled SOS response in bacteria.

PubMed: 26063803
DOI: 10.1074/jbc.M114.620575

実験手法

X-RAY DIFFRACTION (1.94 Å)