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TitleBiochemical and structural studies of conserved maf proteins revealed nucleotide pyrophosphatases with a preference for modified nucleotides.
Journal, issue, pagesChem. Biol., Vol. 20, Page 1386-1398, Year 2013
Publish dateMar 16, 2007 (structure data deposition date)
AuthorsTchigvintsev, A. / Tchigvintsev, D. / Flick, R. / Popovic, A. / Dong, A. / Xu, X. / Brown, G. / Lu, W. / Wu, H. / Cui, H. ...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.
External linksChem. Biol. / PubMed:24210219
MethodsX-ray diffraction
Resolution1.85 - 2.26 Å
Structure data

PDB-2p5x:
Crystal structure of Maf domain of human N-acetylserotonin O-methyltransferase-like protein
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-4heb:
The Crystal structure of Maf protein of Bacillus subtilis
Method: X-RAY DIFFRACTION / Resolution: 2.26 Å

PDB-4jhc:
Crystal structure of the uncharacterized Maf protein YceF from E. coli
Method: X-RAY DIFFRACTION / Resolution: 1.85 Å

PDB-4lu1:
Crystal structure of the uncharacterized Maf protein YceF from E. coli, mutant D69A
Method: X-RAY DIFFRACTION / Resolution: 1.92 Å

Chemicals

ChemComp-PO4:
PHOSPHATE ION

ChemComp-HOH:
WATER

ChemComp-UNX:
Unknown entry

ChemComp-GOL:
GLYCEROL

Source
  • homo sapiens (human)
  • bacillus subtilis (bacteria)
  • escherichia coli (E. coli)
KeywordsCELL CYCLE / asmtl / Structural Genomics / Structural Genomics Consortium / SGC / Bacillus subtilis / Maf proteins / nucleoside triphosphate pyrophosphatase / Maf protein / putative pyrophosphatase / HYDROLASE

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