1uev: Difference between revisions

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-[[Image:1uev.jpg|left|200px]]<br /><applet load="1uev" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1uev, resolution 2.70&Aring;" />
-'''Divergent evolutions of trinucleotide polymerization revealed by an archaeal CCA-adding enzyme structure'''<br />
-==Overview==
+==Divergent evolutions of trinucleotide polymerization revealed by an archaeal CCA-adding enzyme structure==
-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.
+<StructureSection load='1uev' size='340' side='right'caption='[[1uev]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1uev]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UEV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UEV FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1uev FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uev OCA], [https://pdbe.org/1uev PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1uev RCSB], [https://www.ebi.ac.uk/pdbsum/1uev PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1uev ProSAT], [https://www.topsan.org/Proteins/RSGI/1uev TOPSAN]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/CCA_ARCFU CCA_ARCFU] Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate.<ref>PMID:14592988</ref>
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ue/1uev_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1uev ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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==
+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<ref>PMID:14592988</ref>
-UEV 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 MG, CA and ATP 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1UEV OCA].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14592988 14592988]
+</div>
+<div class="pdbe-citations 1uev" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[CCA-adding enzyme 3D structures|CCA-adding enzyme 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Archaeoglobus fulgidus]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: tRNA adenylyltransferase]]
+[[Category: Nureki O]]
-[[Category: Nureki, O.]]
-[[Category: RSGI, RIKEN.Structural.Genomics/Proteomics.Initiative.]]
-[[Category: ATP]]
-[[Category: CA]]
-[[Category: MG]]
-[[Category: riken structural genomics/proteomics initiative]]
-[[Category: rsgi]]
-[[Category: structural genomics]]
-[[Category: transferase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 04:04:45 2007''