1uev: Difference between revisions

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[[Image:1uev.jpg|left|200px]]
{{Seed}}
[[Image:1uev.png|left|200px]]


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{{STRUCTURE_1uev|  PDB=1uev  |  SCENE=  }}  
{{STRUCTURE_1uev|  PDB=1uev  |  SCENE=  }}  


'''Divergent evolutions of trinucleotide polymerization revealed by an archaeal CCA-adding enzyme structure'''
===Divergent evolutions of trinucleotide polymerization revealed by an archaeal CCA-adding enzyme structure===




==Overview==
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CCA-adding enzyme [ATP(CTP):tRNA nucleotidyltransferase], a template-independent RNA polymerase, adds the defined 'cytidine-cytidine-adenosine' sequence onto the 3' end of tRNA. The archaeal CCA-adding enzyme (class I) and eubacterial/eukaryotic CCA-adding enzyme (class II) show little amino acid sequence homology, but catalyze the same reaction in a defined fashion. Here, we present the crystal structures of the class I archaeal CCA-adding enzyme from Archaeoglobus fulgidus, and its complexes with CTP and ATP at 2.0, 2.0 and 2.7 A resolutions, respectively. The geometry of the catalytic carboxylates and the relative positions of CTP and ATP to a single catalytic site are well conserved in both classes of CCA-adding enzymes, whereas the overall architectures, except for the catalytic core, of the class I and class II CCA-adding enzymes are fundamentally different. Furthermore, the recognition mechanisms of substrate nucleotides and tRNA molecules are distinct between these two classes, suggesting that the catalytic domains of class I and class II enzymes share a common origin, and distinct substrate recognition domains have been appended to form the two presently divergent classes.
The line below this paragraph, {{ABSTRACT_PUBMED_14592988}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_14592988}}


==About this Structure==
==About this Structure==
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[[Category: Structural genomic]]
[[Category: Structural genomic]]
[[Category: Transferase]]
[[Category: Transferase]]
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