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4JHC

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

Summary for 4JHC
Entry DOI10.2210/pdb4jhc/pdb
DescriptorMaf-like protein YceF, GLYCEROL, UNKNOWN ATOM OR ION, ... (4 entities in total)
Functional Keywordsmaf protein, putative pyrophosphatase, cell cycle
Biological sourceEscherichia coli
Cellular locationCytoplasm : P0A729
Total number of polymer chains2
Total formula weight48577.05
Authors
Dong, A.,Xu, X.,Cui, H.,Tchigvintsev, A.,Flick, R.,Brown, G.,Popovic, A.,Yakunin, A.F.,Savchenko, A. (deposition date: 2013-03-04, release date: 2013-03-20, Last modification date: 2024-02-28)
Primary citationTchigvintsev, 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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.85 Å)
Structure validation

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건을2025-06-18부터공개중

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