Structural highlights
Publication Abstract from PubMed
The crystal structure of metagenome-derived LC9-RNase H1 was determined. The structure-based mutational analyses indicated that the active site motif of LC9-RNase H1 is altered from DEDD to DEDN. In this motif, the location of the second glutamate residue is moved from alphaA-helix to beta1-strand immediately next to the first aspartate residue, as in the active site of RNase H2. However, the structure and enzymatic properties of LC9-RNase H1 highly resemble those of RNase H1, instead of RNase H2. We propose that LC9-RNase H1 represents bacterial RNases H1 with an atypical DEDN active site motif, which are evolutionarily distinct from those with a typical DEDD active site motif.
Crystal structure of metagenome-derived LC9-RNase H1 with atypical DEDN active site motif.,Nguyen TN, You DJ, Kanaya E, Koga Y, Kanaya S FEBS Lett. 2013 May 2;587(9):1418-23. doi: 10.1016/j.febslet.2013.03.020. Epub, 2013 Mar 20. PMID:23523920[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Nguyen TN, You DJ, Kanaya E, Koga Y, Kanaya S. Crystal structure of metagenome-derived LC9-RNase H1 with atypical DEDN active site motif. FEBS Lett. 2013 May 2;587(9):1418-23. doi: 10.1016/j.febslet.2013.03.020. Epub, 2013 Mar 20. PMID:23523920 doi:10.1016/j.febslet.2013.03.020
