1ou5
From Proteopedia
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| - | [[Image:1ou5.jpg|left|200px]] | + | [[Image:1ou5.jpg|left|200px]] |
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| - | '''Crystal structure of human CCA-adding enzyme''' | + | {{Structure |
| + | |PDB= 1ou5 |SIZE=350|CAPTION= <scene name='initialview01'>1ou5</scene>, resolution 3.40Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= hMtCCA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | }} | ||
| + | |||
| + | '''Crystal structure of human CCA-adding enzyme''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1OU5 is a [ | + | 1OU5 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OU5 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12729736 12729736] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: trna]] | [[Category: trna]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:15:36 2008'' |
Revision as of 11:15, 20 March 2008
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| , resolution 3.40Å | |||||||
|---|---|---|---|---|---|---|---|
| Gene: | hMtCCA (Homo sapiens) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of human CCA-adding enzyme
Contents |
Overview
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.
Disease
Known disease associated with this structure: Deafness, mitochondrial, modifier of OMIM:[610230]
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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