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Publication Abstract from PubMed

The RNA lariat debranching enzyme, Dbr1, is a metallophosphoesterase that cleaves 2'-5' phosphodiester bonds within intronic lariats. Previous reports have indicated that Dbr1 enzymatic activity is supported by diverse metal ions including Ni(2+) , Mn(2+) , Mg(2+) , Fe(2+) , and Zn(2+) . While in initial structures of the Entamoeba histolytica Dbr1 only one of the two catalytic metal-binding sites were observed to be occupied (with a Mn(2+) ion), recent structures determined a Zn(2+) /Fe(2+) heterobinucleation. We solved a high-resolution X-ray crystal structure (1.8 A) of the E. histolytica Dbr1 and determined a Zn(2+) /Mn(2+) occupancy. ICP-AES corroborate this finding, and in vitro debranching assays with fluorescently labeled branched substrates confirm activity.

Crystal structure of the Entamoeba histolytica RNA lariat debranching enzyme EhDbr1 reveals a catalytic Zn(2+) /Mn(2+) heterobinucleation.,Ransey E, Paredes E, Dey SK, Das SR, Heroux A, Macbeth MR FEBS Lett. 2017 Jul;591(13):2003-2010. doi: 10.1002/1873-3468.12677. Epub 2017, Jun 14. PMID:28504306^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.