1uev: Difference between revisions
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|PDB= 1uev |SIZE=350|CAPTION= <scene name='initialview01'>1uev</scene>, resolution 2.70Å | |PDB= 1uev |SIZE=350|CAPTION= <scene name='initialview01'>1uev</scene>, resolution 2.70Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=ATP:ADENOSINE-5'-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> | ||
|ACTIVITY= [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] | |ACTIVITY= <span class='plainlinks'>[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] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1uet|1UET]], [[1ueu|1UEU]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1uev FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uev OCA], [http://www.ebi.ac.uk/pdbsum/1uev PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1uev RCSB]</span> | |||
}} | }} | ||
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[[Category: Nureki, O.]] | [[Category: Nureki, O.]] | ||
[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]] | [[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]] | ||
[[Category: riken structural genomics/proteomics initiative]] | [[Category: riken structural genomics/proteomics initiative]] | ||
[[Category: rsgi]] | [[Category: rsgi]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:09:24 2008'' |
Revision as of 00:09, 31 March 2008
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, resolution 2.70Å | |||||||
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Ligands: | , , | ||||||
Activity: | tRNA adenylyltransferase, with EC number 2.7.7.25 | ||||||
Related: | 1UET, 1UEU
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Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
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
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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