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1ou5

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{{STRUCTURE_1ou5| PDB=1ou5 | SCENE= }}
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'''Crystal structure of human CCA-adding enzyme'''
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===Crystal structure of human CCA-adding enzyme===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_12729736}}
==About this Structure==
==About this Structure==
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[[Category: Polymerase]]
[[Category: Polymerase]]
[[Category: Trna]]
[[Category: Trna]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 05:10:01 2008''

Revision as of 02:10, 29 July 2008

Template:STRUCTURE 1ou5

Crystal structure of human CCA-adding enzyme

Template:ABSTRACT PUBMED 12729736

About this Structure

1OU5 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of the human CCA-adding enzyme: insights into template-independent polymerization., Augustin MA, Reichert AS, Betat H, Huber R, Morl M, Steegborn C, J Mol Biol. 2003 May 16;328(5):985-94. PMID:12729736

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