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

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.

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Genre: Journal Article
Alternative Title : J. Mol. Biol.

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 Creators:
Augustin, M. A.1, Author              
Reichert, A. S., Author
Betat, H., Author
Huber, R.1, Author              
Morl, M., Author
Steegborn, C.1, Author              
Affiliations:
1Huber, Robert / Structure Research, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565155              

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Free keywords: CCA-adding enzyme; class II nucleotidyltransferase; crystal structure; template-independent polymerization; tRNA processing
 Abstract: 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.

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Language(s): eng - English
 Dates: 2003-05-16
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 41374
ISI: 000182767000002
 Degree: -

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Title: Journal of Molecular Biology
  Alternative Title : J. Mol. Biol.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 328 (5) Sequence Number: - Start / End Page: 985 - 994 Identifier: ISSN: 0022-2836