Abstract:
: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 αA-helix to β1-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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Nguyen TN,You DJ,Kanaya E,Koga Y,Kanaya Sdoi
10.1016/j.febslet.2013.03.020subject
Has Abstractpub_date
2013-05-02 00:00:00pages
1418-23issue
9eissn
0014-5793issn
1873-3468pii
S0014-5793(13)00231-7journal_volume
587pub_type
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