4OHY

C. Elegans Clp1 bound to ssRNA dinucleotide GC, AMP-PNP, and Mg2+(inhibited substrate bound state)

4OHY の概要

• エントリーDOI: 10.2210/pdb4ohy/pdb
• 関連するPDBエントリー: 4OHV 4OHW 4OHX 4OHZ 4OI0 4OI1 4OI2
• 分子名称: Protein clpf-1, RNA (5'-R(*GP*C)-3'), PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, ... (6 entities in total)
• 機能のキーワード: polynucleotide kinase, rna binding protein-rna complex, rna binding protein/rna
• 由来する生物種: Caenorhabditis elegans (nematode); 詳細
• 細胞内の位置: Nucleus : P52874
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 49486.87

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: 2024-02-28)

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 Å)