4JHC

Crystal structure of the uncharacterized Maf protein YceF from E. coli

4JHC の概要

• エントリーDOI: 10.2210/pdb4jhc/pdb
• 分子名称: Maf-like protein YceF, GLYCEROL, UNKNOWN ATOM OR ION, ... (4 entities in total)
• 機能のキーワード: maf protein, putative pyrophosphatase, cell cycle
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cytoplasm : P0A729
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 48577.05

構造登録者

Dong, A.,Xu, X.,Cui, H.,Tchigvintsev, A.,Flick, R.,Brown, G.,Popovic, A.,Yakunin, A.F.,Savchenko, A. (登録日: 2013-03-04, 公開日: 2013-03-20, 最終更新日: 2024-02-28)

主引用文献

Tchigvintsev, A.,Tchigvintsev, D.,Flick, R.,Popovic, A.,Dong, A.,Xu, X.,Brown, G.,Lu, W.,Wu, H.,Cui, H.,Dombrowski, L.,Joo, J.C.,Beloglazova, N.,Min, J.,Savchenko, A.,Caudy, A.A.,Rabinowitz, J.D.,Murzin, A.G.,Yakunin, A.F.
Biochemical and structural studies of conserved maf proteins revealed nucleotide pyrophosphatases with a preference for modified nucleotides.
Chem.Biol., 20:1386-1398, 2013

PubMed Abstract: Maf (for multicopy associated filamentation) proteins represent a large family of conserved proteins implicated in cell division arrest but whose biochemical activity remains unknown. Here, we show that the prokaryotic and eukaryotic Maf proteins exhibit nucleotide pyrophosphatase activity against 5-methyl-UTP, pseudo-UTP, 5-methyl-CTP, and 7-methyl-GTP, which represent the most abundant modified bases in all organisms, as well as against canonical nucleotides dTTP, UTP, and CTP. Overexpression of the Maf protein YhdE in E. coli cells increased intracellular levels of dTMP and UMP, confirming that dTTP and UTP are the in vivo substrates of this protein. Crystal structures and site-directed mutagenesis of Maf proteins revealed the determinants of their activity and substrate specificity. Thus, pyrophosphatase activity of Maf proteins toward canonical and modified nucleotides might provide the molecular mechanism for a dual role of these proteins in cell division arrest and house cleaning.

PubMed: 24210219
DOI: 10.1016/j.chembiol.2013.09.011

実験手法

X-RAY DIFFRACTION (1.85 Å)