5A2V

Crystal structure of mtPAP in Apo form

5A2V の概要

• エントリーDOI: 10.2210/pdb5a2v/pdb
• 関連するPDBエントリー: 5A2W 5A2X 5A2Y 5A2Z 5A30
• 分子名称: MITOCHONDRIAL PROTEIN, CHLORIDE ION (3 entities in total)
• 機能のキーワード: unknown function
• 由来する生物種: GALLUS GALLUS (CHICKEN)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 126050.00

構造登録者

Lapkouski, M.,Hallberg, B.M. (登録日: 2015-05-26, 公開日: 2015-09-09, 最終更新日: 2024-05-08)

主引用文献

Lapkouski, M.,Hallberg, B.M.
Structure of Mitochondrial Poly(A) RNA Polymerase Reveals the Structural Basis for Dimerization, ATP Selectivity and the Spax4 Disease Phenotype.
Nucleic Acids Res., 43:9065-, 2015

PubMed Abstract: Polyadenylation, performed by poly(A) polymerases (PAPs), is a ubiquitous post-transcriptional modification that plays key roles in multiple aspects of RNA metabolism. Although cytoplasmic and nuclear PAPs have been studied extensively, the mechanism by which mitochondrial PAP (mtPAP) selects adenosine triphosphate over other nucleotides is unknown. Furthermore, mtPAP is unique because it acts as a dimer. However, mtPAP's dimerization requirement remains enigmatic. Here, we show the structural basis for mtPAP's nucleotide selectivity, dimerization and catalysis. Our structures reveal an intricate dimerization interface that features an RNA-recognition module formed through strand complementation. Further, we propose the structural basis for the N478D mutation that drastically reduces the length of poly(A) tails on mitochondrial mRNAs in patients with spastic ataxia 4 (SPAX4), a severe and progressive neurodegenerative disease.

PubMed: 26319014
DOI: 10.1093/NAR/GKV861

実験手法

X-RAY DIFFRACTION (1.82 Å)