Crystal structure of yeast YER010Cp, a knotable member of the RraA protein family.

@article{Leulliot2005CrystalSO,
  title={Crystal structure of yeast YER010Cp, a knotable member of the RraA protein family.},
  author={Nicolas Leulliot and Sophie Quevillon-Ch{\'e}ruel and Marc Graille and Marc Schiltz and Karine Blondeau and Jo{\"e}l Janin and Herman van Tilbeurgh},
  journal={Protein science : a publication of the Protein Society},
  year={2005},
  volume={14 10},
  pages={
          2751-8
        }
}
We present here the structure of Yer010c protein of unknown function, solved by Multiple Anomalous Diffraction and revealing a common fold and oligomerization state with proteins of the regulator of ribonuclease activity A (RraA) family. In Escherichia coli, RraA has been shown to regulate the activity of ribonuclease E by direct interaction. The absence of ribonuclease E in yeast suggests a different function for this family member in this organism. Yer010cp has a few supplementary secondary… CONTINUE READING
BETA