4E7X

Structural Basis for the Activity of a Cytoplasmic RNA Terminal U-transferase

4E7X の概要

• エントリーDOI: 10.2210/pdb4e7x/pdb
• 関連するPDBエントリー: 4E80 4E8F
• 分子名称: Poly(A) RNA polymerase protein cid1, ACETATE ION (3 entities in total)
• 機能のキーワード: beta polymerase-like nucleotidyl transferase, terminal uridine transferase, utp, rna, cytoplasmic, transferase
• 由来する生物種: Schizosaccharomyces pombe 972h- (Fission yeast)
• 細胞内の位置: Cytoplasm : O13833
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 185515.41

構造登録者

Yates, L.A.,Fleurdepine, S.,Rissland, O.S.,DeColibus, L.,Harlos, K.,Norbury, C.J.,Gilbert, R.J.C. (登録日: 2012-03-19, 公開日: 2012-07-04, 最終更新日: 2024-02-28)

主引用文献

Yates, L.A.,Fleurdepine, S.,Rissland, O.S.,De Colibus, L.,Harlos, K.,Norbury, C.J.,Gilbert, R.J.
Structural basis for the activity of a cytoplasmic RNA terminal uridylyl transferase.
Nat.Struct.Mol.Biol., 19:782-787, 2012

PubMed Abstract: Cytoplasmic terminal uridylyl transferases comprise a conserved family of enzymes that negatively regulate the stability or biological activity of a variety of eukaryotic RNAs, including mRNAs and tumor-suppressor let-7 microRNAs. Here we describe crystal structures of the Schizosaccharomyces pombe cytoplasmic terminal uridylyl transferase Cid1 in two apo conformers and bound to UTP. We demonstrate that a single histidine residue, conserved in mammalian Cid1 orthologs, is responsible for discrimination between UTP and ATP. We also describe a new high-affinity RNA substrate-binding mechanism of Cid1, which is essential for enzymatic activity and is mediated by three basic patches across the surface of the enzyme. Overall, our structures provide a basis for understanding the activity of Cid1 and a mechanism of UTP selectivity conserved in its human orthologs, suggesting potential implications for anticancer drug design.

PubMed: 22751018
DOI: 10.1038/nsmb.2329

実験手法

X-RAY DIFFRACTION (3.2 Å)