1miw

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<StructureSection load='1miw' size='340' side='right'caption='[[1miw]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
<StructureSection load='1miw' size='340' side='right'caption='[[1miw]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1miw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_12980 Atcc 12980]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MIW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MIW FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1miw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MIW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MIW FirstGlance]. <br>
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</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=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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<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=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1miv|1miv]], [[1miy|1miy]]</div></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1miw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1miw OCA], [https://pdbe.org/1miw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1miw RCSB], [https://www.ebi.ac.uk/pdbsum/1miw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1miw ProSAT]</span></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=1miw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1miw OCA], [https://pdbe.org/1miw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1miw RCSB], [https://www.ebi.ac.uk/pdbsum/1miw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1miw ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CCA_GEOSE CCA_GEOSE]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=1miw ConSurf].
</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=1miw ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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CCA-adding enzymes polymerize CCA onto the 3' terminus of immature tRNAs without using a nucleic acid template. The 3.0 A resolution crystal structures of the CCA-adding enzyme from Bacillus stearothermophilus and its complexes with ATP or CTP reveal a seahorse-shaped subunit consisting of four domains: head, neck, body, and tail. The head is structurally homologous to the palm domain of DNA polymerase beta but has additional structural features and functions. The neck, body, and tail represent new protein folding motifs. The neck provides a specific template for the incoming ATP or CTP, whereas the body and tail may bind tRNA. Each subunit has one active site capable of switching its base specificity between ATP and CTP, an important component of the CCA-adding mechanism.
 
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Crystal structures of the Bacillus stearothermophilus CCA-adding enzyme and its complexes with ATP or CTP.,Li F, Xiong Y, Wang J, Cho HD, Tomita K, Weiner AM, Steitz TA Cell. 2002 Dec 13;111(6):815-24. PMID:12526808<ref>PMID:12526808</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 1miw" style="background-color:#fffaf0;"></div>
 
==See Also==
==See Also==
*[[CCA-adding enzyme 3D structures|CCA-adding enzyme 3D structures]]
*[[CCA-adding enzyme 3D structures|CCA-adding enzyme 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Atcc 12980]]
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[[Category: Geobacillus stearothermophilus]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Cho, H D]]
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[[Category: Cho HD]]
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[[Category: Li, F]]
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[[Category: Li F]]
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[[Category: Steitz, T A]]
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[[Category: Steitz TA]]
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[[Category: Wang, J]]
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[[Category: Wang J]]
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[[Category: Weiner, A M]]
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[[Category: Weiner AM]]
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[[Category: Xiong, Y]]
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[[Category: Xiong Y]]
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[[Category: Cca-adding enzyme]]
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[[Category: Transferase]]
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[[Category: Translation]]
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[[Category: Trna nucleotidyltransferase]]
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Revision as of 08:36, 10 April 2024

Crystal structure of Bacillus stearothermophilus CCA-adding enzyme in complex with ATP

PDB ID 1miw

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