The crystal structure of M. leprae ML2640c defines a large family of putative S-adenosylmethionine-dependent methyltransferases in mycobacteria.

@article{Graa2007TheCS,
  title={The crystal structure of M. leprae ML2640c defines a large family of putative S-adenosylmethionine-dependent methyltransferases in mycobacteria.},
  author={Mart{\'i}n Gra{\~n}a and Ahmed Haouz and Alejandro Buschiazzo and Isabelle Miras and Annemarie Wehenkel and Vincent Bondet and William Shepard and Francis Schaeffer and Stewart T Cole and Pedro M Alzari},
  journal={Protein science : a publication of the Protein Society},
  year={2007},
  volume={16 9},
  pages={1896-904}
}
Mycobacterium leprae protein ML2640c belongs to a large family of conserved hypothetical proteins predominantly found in mycobacteria, some of them predicted as putative S-adenosylmethionine (AdoMet)-dependent methyltransferases (MTase). As part of a Structural Genomics initiative on conserved hypothetical proteins in pathogenic mycobacteria, we have determined the structure of ML2640c in two distinct crystal forms. As expected, ML2640c has a typical MTase core domain and binds the methyl donor… CONTINUE READING

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