PDBsum entry 4jhc

Cell cycle

PDB id: 4jhc

Contents

Protein chains

192 a.a.

182 a.a.

Ligands

GOL ×3

UNX ×12

Waters ×189

PDB id:

4jhc

Name:

Cell cycle

Title:

Crystal structure of the uncharacterized maf protein ycef from e. Coli

Structure:

Maf-like protein ycef. Chain: a, b. Engineered: yes

Source:

Escherichia coli. Organism_taxid: 83333. Strain: k12. Gene: ycef, b1087, jw5155. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

1.85Å R-factor: 0.195 R-free: 0.247

Authors:

A.Dong,X.Xu,H.Cui,A.Tchigvintsev,R.Flick,G.Brown,A.Popovic, A.F.Yakunin,A.Savchenko

Key ref:

A.Tchigvintsev et al. (2013). Biochemical and structural studies of conserved Maf proteins revealed nucleotide pyrophosphatases with a preference for modified nucleotides. Chem Biol, 20, 1386-1398. PubMed id: 24210219 DOI: 10.1016/j.chembiol.2013.09.011

Date:

04-Mar-13 Release date: 20-Mar-13

Protein chain

P0A729  (YCEF_ECOLI) -  7-methyl-GTP pyrophosphatase from Escherichia coli (strain K12)

Seq: 194 a.a.

Struc: 192 a.a.

Protein chain

P0A729  (YCEF_ECOLI) -  7-methyl-GTP pyrophosphatase from Escherichia coli (strain K12)

Seq: 194 a.a.

Struc: 182 a.a.

Enzyme reactions

• Enzyme class: Chains A, B: E.C.3.6.1.- - ?????

DOI no: 10.1016/j.chembiol.2013.09.011

Chem Biol 20:1386-1398 (2013)

PubMed id: 24210219

Biochemical and structural studies of conserved Maf proteins revealed nucleotide pyrophosphatases with a preference for modified nucleotides.

A.Tchigvintsev, D.Tchigvintsev, R.Flick, A.Popovic, A.Dong, X.Xu, G.Brown, W.Lu, H.Wu, H.Cui, L.Dombrowski, J.C.Joo, N.Beloglazova, J.Min, A.Savchenko, A.A.Caudy, J.D.Rabinowitz, A.G.Murzin, A.F.Yakunin.

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.