@article{RedelbergerSedukGenestetal.2011,
  author    = {Redelberger, David and Seduk, Farida and Genest, Olivier and Mejean, Vincent and Leimk{\"u}hler, Silke and Iobbi-Nivol, Chantal},
  title     = {YcdY Protein of Escherichia coli, an Atypical Member of the TorD Chaperone Family},
  series = {Journal of bacteriology},
  volume    = {193},
  journal   = {Journal of bacteriology},
  number    = {23},
  publisher = {American Society for Microbiology},
  address   = {Washington},
  issn      = {0021-9193},
  doi       = {10.1128/JB.05927-11},
  pages     = {6512 -- 6516},
  year      = {2011},
  abstract  = {The TorD family of specific chaperones is divided into four subfamilies dedicated to molybdoenzyme biogenesis and a fifth one, exemplified by YcdY of Escherichia coli, for which no defined partner has been identified so far. We propose that YcdY is the chaperone of YcdX, a zinc protein involved in the swarming motility process of E. coli, since YcdY interacts with YcdX and increases its activity in vitro.},
  language  = {en}
}
@article{NeumannSedukIobbiNivoletal.2011,
  author    = {Neumann, Meina and Seduk, Farida and Iobbi-Nivol, Chantal and Leimk{\"u}hler, Silke},
  title     = {Molybdopterin Dinucleotide Biosynthesis in Escherichia coli identification of amino acid residues of molybdopterin dinucleotide transferases that determine specificity for binding of guanine or cytosine nucleotides},
  series = {The journal of biological chemistry},
  volume    = {286},
  journal   = {The journal of biological chemistry},
  number    = {2},
  publisher = {American Society for Biochemistry and Molecular Biology},
  address   = {Bethesda},
  issn      = {0021-9258},
  doi       = {10.1074/jbc.M110.155671},
  pages     = {1400 -- 1408},
  year      = {2011},
  abstract  = {The molybdenum cofactor is modified by the addition of GMP or CMP to the C4' phosphate of molybdopterin forming the molybdopterin guanine dinucleotide or molybdopterin cytosine dinucleotide cofactor, respectively. The two reactions are catalyzed by specific enzymes as follows: the GTP: molybdopterin guanylyltransferase MobA and the CTP: molybdopterin cytidylyltransferase MocA. Both enzymes show 22\% amino acid sequence identity and are specific for their respective nucleotides. Crystal structure analysis of MobA revealed two conserved motifs in the N-terminal domain of the protein involved in binding of the guanine base. Based on these motifs, we performed site-directed mutagenesis studies to exchange the amino acids to the sequence found in the paralogue MocA. Using a fully defined in vitro system, we showed that the exchange of five amino acids was enough to obtain activity with both GTP and CTP in either MocA or MobA. Exchange of the complete N-terminal domain of each protein resulted in the total inversion of nucleotide specificity activity, showing that the N-terminal domain determines nucleotide recognition and binding. Analysis of protein-protein interactions showed that the C-terminal domain of either MocA or MobA determines the specific binding to the respective acceptor protein.},
  language  = {en}
}