5UKI

Mn2+ and Zn2+ requirements for the lariat debranching enzyme, Dbr1

5UKI の概要

• エントリーDOI: 10.2210/pdb5uki/pdb
• 分子名称: RNA lariat debranching enzyme, putative, ZINC ION, MANGANESE (II) ION, ... (4 entities in total)
• 機能のキーワード: debranching, metal ions, rna, hydrolase
• 由来する生物種: Entamoeba histolytica
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 40702.86

構造登録者

Macbeth, M.R.,Ransey, L. (登録日: 2017-01-22, 公開日: 2018-02-21, 最終更新日: 2024-03-06)

主引用文献

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

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: 28504306
DOI: 10.1002/1873-3468.12677

実験手法

X-RAY DIFFRACTION (1.8 Å)