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

Title data

Augustin, Martin A. ; Reichert, Andreas S. ; Betat, Heike ; Huber, Robert ; Mörl, Mario ; Steegborn, Clemens:
Crystal structure of the human CCA-adding enzyme: insights into template-independent polymerization.
In: Journal of Molecular Biology. Vol. 328 (16 May 2003) Issue 5 . - pp. 985-994.
ISSN 0022-2836
DOI: https://doi.org/10.1016/S0022-2836(03)00381-4

Abstract in another language

All tRNA molecules carry the invariant sequence CCA at their 3'-terminus for amino acid attachment. The post-transcriptional 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.

Further data

Item Type: Article in a journal
Refereed: Yes
Additional notes: PubMed-ID: 12729736
Institutions of the University: Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biochemistry > Chair Biochemistry - Univ.-Prof. Dr. Clemens Steegborn
Faculties
Faculties > Faculty of Biology, Chemistry and Earth Sciences
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biochemistry
Result of work at the UBT: No
DDC Subjects: 500 Science > 540 Chemistry
Date Deposited: 13 Apr 2015 11:07
Last Modified: 13 Apr 2015 11:07
URI: https://eref.uni-bayreuth.de/id/eprint/10111