1uet
From Proteopedia
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|PDB= 1uet |SIZE=350|CAPTION= <scene name='initialview01'>1uet</scene>, resolution 2.00Å | |PDB= 1uet |SIZE=350|CAPTION= <scene name='initialview01'>1uet</scene>, resolution 2.00Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> | + | |LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</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=[[1ueu|1UEU]], [[1uev|1UEV]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1uet FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uet OCA], [http://www.ebi.ac.uk/pdbsum/1uet PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1uet 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: ACT]] | ||
| - | [[Category: CA]] | ||
| - | [[Category: MG]] | ||
[[Category: riken structural genomics/proteomics initiative]] | [[Category: riken structural genomics/proteomics initiative]] | ||
[[Category: rsgi]] | [[Category: rsgi]] | ||
| Line 33: | Line 33: | ||
[[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 21:09, 30 March 2008
| |||||||
| , resolution 2.00Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Activity: | tRNA adenylyltransferase, with EC number 2.7.7.25 | ||||||
| Related: | 1UEU, 1UEV
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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.
About this Structure
1UET is a Single protein structure of sequence from Archaeoglobus fulgidus. Full crystallographic information is available from OCA.
Reference
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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