4OI4

Protein complex of Clp1 bound to ATP and Mg2+ with Pcf11deltaN454deltaC563 of S. cerevisiae

4OI4 の概要

• エントリーDOI: 10.2210/pdb4oi4/pdb
• 関連するPDBエントリー: 2NPI
• 分子名称: mRNA cleavage and polyadenylation factor CLP1, Protein PCF11, ADENOSINE-5'-TRIPHOSPHATE, ... (6 entities in total)
• 機能のキーワード: polynucleotide kinase, clp1, pcf11, cleavage factor ia, 3'-end mrna processing, transcription
• 由来する生物種: Saccharomyces cerevisiae (Baker's yeast); 詳細
• 細胞内の位置: Nucleus : Q08685 P39081
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 142435.55

構造登録者

Dikfidan, A.,Loll, B.,Zeymer, C.,Clausen, T.,Meinhart, A. (登録日: 2014-01-18, 公開日: 2014-05-14, 最終更新日: 2023-09-20)

主引用文献

Dikfidan, A.,Loll, B.,Zeymer, C.,Magler, I.,Clausen, T.,Meinhart, A.
RNA specificity and regulation of catalysis in the eukaryotic polynucleotide kinase clp1.
Mol.Cell, 54:975-986, 2014

PubMed Abstract: RNA-specific polynucleotide kinases of the Clp1 subfamily are key components of various RNA maturation pathways. However, the structural basis explaining their substrate specificity and the enzymatic mechanism is elusive. Here, we report crystal structures of Clp1 from Caenorhabditis elegans (ceClp1) in a number of nucleotide- and RNA-bound states along the reaction pathway. The combined structural and biochemical analysis of ceClp1 elucidates the RNA specificity and lets us derive a general model for enzyme catalysis of RNA-specific polynucleotide kinases. We identified an RNA binding motif referred to as "clasp" as well as a conformational switch that involves the essential Walker A lysine (Lys127) and regulates the enzymatic activity of ceClp1. Structural comparison with other P loop proteins, such as kinases, adenosine triphosphatases (ATPases), and guanosine triphosphatases (GTPases), suggests that the observed conformational switch of the Walker A lysine is a broadly relevant mechanistic feature.

PubMed: 24813946
DOI: 10.1016/j.molcel.2014.04.005

実験手法

X-RAY DIFFRACTION (2.4 Å)