4YIX

Structure of MRB1590 bound to ADP

4YIX の概要

• エントリーDOI: 10.2210/pdb4yix/pdb
• 関連するPDBエントリー: 4YIY
• 分子名称: Uncharacterized protein, MAGNESIUM ION, MERCURY (II) ION, ... (5 entities in total)
• 機能のキーワード: krna editing, mrb1590, atpase, rna binding, rna binding protein
• 由来する生物種: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 75503.84

構造登録者

Shaw, P.L.R.,Schumacher, M.A. (登録日: 2015-03-02, 公開日: 2015-08-12, 最終更新日: 2024-02-28)

主引用文献

Shaw, P.L.,McAdams, N.M.,Hast, M.A.,Ammerman, M.L.,Read, L.K.,Schumacher, M.A.
Structures of the T. brucei kRNA editing factor MRB1590 reveal unique RNA-binding pore motif contained within an ABC-ATPase fold.
Nucleic Acids Res., 43:7096-7109, 2015

PubMed Abstract: Kinetoplastid RNA (kRNA) editing is a process that creates translatable mitochondrial mRNA transcripts from cryptogene encoded RNAs and is unique for kinetoplastids, such as Trypanosoma brucei. In addition to the catalytic 20S editosome, multiple accessory proteins are required for this conversion. Recently, the multiprotein mitochondrial RNA binding complex 1 (MRB1) has emerged as a key player in this process. MRB1 consists of six core proteins but makes dynamic interactions with additional accessory proteins. Here we describe the characterization of one such factor, the 72 kDa MRB1590 protein. In vivo experiments indicate a role for MRB1590 in editing mitochondrial mRNA transcripts, in particular the transcript encoding the ATP synthase subunit 6 (A6). Structural studies show that MRB1590 is dimeric and contains a central ABC-ATPase fold embedded between novel N- and C-terminal regions. The N-terminal domains combine to create a basic pore and biochemical studies indicate residues in this region participate in RNA binding. Structures capturing distinct MRB1590 conformations reveal that the RNA binding pore adopts closed and open states, with the latter able to accommodate RNA. Based on these findings, implications for MRB1590 function are discussed.

PubMed: 26117548
DOI: 10.1093/nar/gkv647

実験手法

X-RAY DIFFRACTION (2.6 Å)