1uet: Difference between revisions
New page: left|200px<br /><applet load="1uet" size="450" color="white" frame="true" align="right" spinBox="true" caption="1uet, resolution 2.00Å" /> '''Divergent evolutions... |
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[[Image:1uet.jpg|left|200px]]<br /><applet load="1uet" size=" | [[Image:1uet.jpg|left|200px]]<br /><applet load="1uet" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1uet, resolution 2.00Å" /> | caption="1uet, resolution 2.00Å" /> | ||
'''Divergent evolutions of trinucleotide polymerization revealed by an archaeal CCA-adding enzyme structure'''<br /> | '''Divergent evolutions of trinucleotide polymerization revealed by an archaeal CCA-adding enzyme structure'''<br /> | ||
==Overview== | ==Overview== | ||
CCA-adding enzyme [ATP(CTP):tRNA nucleotidyltransferase], a | 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. | ||
==About this Structure== | ==About this Structure== | ||
1UET is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus] with ACT, CA and MG as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/tRNA_adenylyltransferase tRNA adenylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.25 2.7.7.25] Full crystallographic information is available from [http:// | 1UET is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus] with <scene name='pdbligand=ACT:'>ACT</scene>, <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=MG:'>MG</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/tRNA_adenylyltransferase tRNA adenylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.25 2.7.7.25] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UET OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: tRNA adenylyltransferase]] | [[Category: tRNA adenylyltransferase]] | ||
[[Category: Nureki, O.]] | [[Category: Nureki, O.]] | ||
[[Category: RSGI, RIKEN | [[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]] | ||
[[Category: ACT]] | [[Category: ACT]] | ||
[[Category: CA]] | [[Category: CA]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:23:45 2008'' | ||
Revision as of 16:23, 21 February 2008
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Divergent evolutions of trinucleotide polymerization revealed by an archaeal CCA-adding enzyme structure
OverviewOverview
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.
About this StructureAbout this Structure
1UET is a Single protein structure of sequence from Archaeoglobus fulgidus with , and as ligands. Active as tRNA adenylyltransferase, with EC number 2.7.7.25 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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