Ribonuclease H1 (2QK9)
It’s my PhD protein! RNase H is an enzyme that cleaves DNA-RNA hybrids that is found in all domains of life. RNases H from mesophilic and thermophilic bacteria were among the first homologous structures solved from organisms adapted to different temperatures and are structurally very similar despite large differences in enzymatic activity. My work used molecular dynamics simulations to interpret NMR measurements of these proteins’ internal dynamics to better understand the relationship between motion, function, and thermal adaptation.
The PDB code cited above (2QK9) is that of the human RNase H homolog, which was solved in the presence of a hybrid substrate.
RNase H is essential in higher eukaryotes, so everyone reading this has a functional one. It is also essential for the proliferation of retroviruses, making selective inhibitors of the retroviral RNase H domain a potential drug target for novel HIV treatments.
The attached photo is the human RNase H 3D printed with Shapeways. —Kate Stafford