5UKI
Mn2+ and Zn2+ requirements for the lariat debranching enzyme, Dbr1
Summary for 5UKI
| Entry DOI | 10.2210/pdb5uki/pdb |
| Descriptor | RNA lariat debranching enzyme, putative, ZINC ION, MANGANESE (II) ION, ... (4 entities in total) |
| Functional Keywords | debranching, metal ions, rna, hydrolase |
| Biological source | Entamoeba histolytica |
| Total number of polymer chains | 1 |
| Total formula weight | 40702.86 |
| Authors | Macbeth, M.R.,Ransey, L. (deposition date: 2017-01-22, release date: 2018-02-21, Last modification date: 2024-03-06) |
| Primary citation | Ransey, E.,Paredes, E.,Dey, S.K.,Das, S.R.,Heroux, A.,Macbeth, M.R. Crystal structure of the Entamoeba histolytica RNA lariat debranching enzyme EhDbr1 reveals a catalytic Zn2+/Mn2+heterobinucleation. FEBS Lett., 591:2003-2010, 2017 Cited by PubMed Abstract: 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 , Mn , Mg , Fe , and Zn . 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 ion), recent structures determined a Zn /Fe heterobinucleation. We solved a high-resolution X-ray crystal structure (1.8 Å) of the E. histolytica Dbr1 and determined a Zn /Mn occupancy. ICP-AES corroborate this finding, and in vitro debranching assays with fluorescently labeled branched substrates confirm activity. PubMed: 28504306DOI: 10.1002/1873-3468.12677 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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