The crystal structure of the Escherichia coli MobA protein provides insight into molybdopterin guanine dinucleotide biosynthesis.

@article{Lake2000TheCS,
  title={The crystal structure of the Escherichia coli MobA protein provides insight into molybdopterin guanine dinucleotide biosynthesis.},
  author={Michael W. Lake and Carrie A. Temple and Krishnakumar Rajagopalan and Hermann Schindelin},
  journal={The Journal of biological chemistry},
  year={2000},
  volume={275 51},
  pages={40211-7}
}
The molybdenum cofactor (Moco) is found in a variety of enzymes present in all phyla and comprises a family of related molecules containing molybdopterin (MPT), a tricyclic pyranopterin with a cis-dithiolene group, as the invariant essential moiety. MPT biosynthesis involves a conserved pathway, but some organisms perform additional reactions that modify MPT. In eubacteria, the cofactor is often present in a dinucleotide form combining MPT and a purine or pyrimidine nucleotide via a… CONTINUE READING
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