4ibn
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Crystal structure of LC9-RNase H1, a type 1 RNase H with the type 2 active-site motif
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Structural highlights
FunctionPublication Abstract from PubMedThe 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 AlsoReferences
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This page was last modified 14:13, 8 November 2023.