RNA specificity and regulation of catalysis in the eukaryotic polynucleotide kinase clp1.
作者： Aytac Dikfidan , Bernhard Loll , Cathleen Zeymer , Iris Magler , Tim Clausen
DOI: 10.1016/J.MOLCEL.2014.04.005
关键词: RNA editing 、 Biology 、 Walker motifs 、 Polynucleotide Kinase 、 Biochemistry 、 Degradosome 、 Transcription (biology) 、 RNA-binding protein 、 Polynucleotide 、 RNA
摘要: Summary RNA-specific polynucleotide kinases of the Clp1 subfamily are key components various RNA maturation pathways. However, structural basis explaining their substrate specificity and enzymatic mechanism is elusive. Here, we report crystal structures from Caenorhabditis elegans (ceClp1) in a number nucleotide- RNA-bound states along reaction pathway. The combined biochemical analysis ceClp1 elucidates lets us derive general model for enzyme catalysis kinases. We identified an binding motif referred to as "clasp" well conformational switch that involves essential Walker A lysine (Lys127) regulates activity ceClp1. Structural comparison with other P loop proteins, such kinases, adenosine triphosphatases (ATPases), guanosine (GTPases), suggests observed broadly relevant mechanistic feature.
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