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4LU1

Crystal structure of the uncharacterized Maf protein YceF from E. coli, mutant D69A

4LU1 の概要
エントリーDOI10.2210/pdb4lu1/pdb
分子名称Maf-like protein YceF, UNKNOWN ATOM OR ION (3 entities in total)
機能のキーワードmaf protein, putative pyrophosphatase, structural genomics, structural genomics consortium, sgc, hydrolase
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48212.75
構造登録者
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
Cited by
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
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.92 Å)
構造検証レポート
Validation report summary of 4lu1
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-02-04に公開中

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