1uev: Difference between revisions

Revision as of 23:23, 27 July 2008

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File:1uev.png

Template:STRUCTURE 1uev

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

Template:ABSTRACT PUBMED 14592988

About this StructureAbout this Structure

1UEV is a Single protein structure of sequence from Archaeoglobus fulgidus. Full crystallographic information is available from OCA.

ReferenceReference

Divergent evolutions of trinucleotide polymerization revealed by an archaeal CCA-adding enzyme structure., Okabe M, Tomita K, Ishitani R, Ishii R, Takeuchi N, Arisaka F, Nureki O, Yokoyama S, EMBO J. 2003 Nov 3;22(21):5918-27. PMID:14592988

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OCA

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-'''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==
+<!--
-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
+(as it appears on PubMed at http://www.pubmed.gov), where 14592988 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_14592988}}
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 [[Category: Structural genomic]]
 [[Category: Transferase]]
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