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Crystal structure of the human CCA-adding enzyme: Insights into template-independent polymerization

MPG-Autoren
http://pubman.mpdl.mpg.de/cone/persons/resource/persons77690

Augustin,  M. A.
Huber, Robert / Structure Research, Max Planck Institute of Biochemistry, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons78142

Huber,  R.
Huber, Robert / Structure Research, Max Planck Institute of Biochemistry, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons78742

Steegborn,  C.
Huber, Robert / Structure Research, Max Planck Institute of Biochemistry, Max Planck Society;

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Zitation

Augustin, M. A., Reichert, A. S., Betat, H., Huber, R., Morl, M., & Steegborn, C. (2003). Crystal structure of the human CCA-adding enzyme: Insights into template-independent polymerization. Journal of Molecular Biology, 328(5), 985-994.


Zitierlink: http://hdl.handle.net/11858/00-001M-0000-0010-6BE7-F
Zusammenfassung
All tRNA molecules carry the invariant sequence CCA at their 3'-terminus for amino acid attachment. The post-transcriptimal addition of CCA is carried out by ATP(CTP):tRNA nucleotidyltransferase, also called CCase. This enzyme catalyses a unique template-independent but sequence-specific nucleotide polymerization reaction. In order to reveal the molecular mechanism of this activity, we solved the crystal structure of human CCase by single isomorphous replacement. The structure reveals a four domain architecture with a cluster of conserved residues forming a positively charged cleft between the first two domains. Structural homology of the N-terminal CCase domain to other nucleotidyltransferases could be exploited for modeling a tRNA-substrate complex. The model places the tRNA 3'-end into the N-terminal nucleotidyltransferase site, close to a patch of conserved residues that provide the binding sites for CTP and ATP Based on our results, we introduce a corkscrew model for CCA addition that includes a fixed active site and a traveling tRNA-binding region formed by flexible parts of the protein. (C) 2003 Elsevier Science Ltd. All rights reserved.