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  RNA specificity and regulation of catalysis in the eukaryotic polynucleotide kinase clp1

Dikfidan, A., Loll, B., Zeymer, C., Magler, I., Clausen, T., & Meinhart, A. (2014). RNA specificity and regulation of catalysis in the eukaryotic polynucleotide kinase clp1. Molecular Cell, 54(6), 975-986. doi:10.1016/j.molcel.2014.04.005.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0019-CE24-2 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0019-CE25-F
Genre: Journal Article

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Dikfidan, Aytac1, Author              
Loll, Bernhard1, Author              
Zeymer, Cathleen1, Author              
Magler, Iris1, Author              
Clausen , Tim, Author
Meinhart, Anton1, Author              
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1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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 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.

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Language(s): eng - English
 Dates: 2014-01-272013-11-192014-04-032014-05-082014-06-19
 Publication Status: Published in print
 Pages: 12
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/j.molcel.2014.04.005
Other: 7988
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Title: Molecular Cell
Source Genre: Journal
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Pages: - Volume / Issue: 54 (6) Sequence Number: - Start / End Page: 975 - 986 Identifier: ISSN: 1097-2765
CoNE: https://pure.mpg.de/cone/journals/resource/954925610929