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4HEB

The Crystal structure of Maf protein of Bacillus subtilis

4HEB の概要
エントリーDOI10.2210/pdb4heb/pdb
関連するPDBエントリー2P5X
分子名称Septum formation protein Maf, UNKNOWN ATOM OR ION (3 entities in total)
機能のキーワードbacillus subtilis, maf proteins, nucleoside triphosphate pyrophosphatase, structural genomics, structural genomics consortium, sgc, cell cycle
由来する生物種Bacillus subtilis
細胞内の位置Cytoplasm (Potential): Q02169
タンパク質・核酸の鎖数2
化学式量合計47509.96
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 (2.26 Å)
構造検証レポート
Validation report summary of 4heb
検証レポート(詳細版)ダウンロードをダウンロード

246905

件を2025-12-31に公開中

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