1ou5

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[[Image:1ou5.jpg|left|200px]]
 
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{{Structure
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==Crystal structure of human CCA-adding enzyme==
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|PDB= 1ou5 |SIZE=350|CAPTION= <scene name='initialview01'>1ou5</scene>, resolution 3.40&Aring;
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<StructureSection load='1ou5' size='340' side='right'caption='[[1ou5]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[1ou5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OU5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OU5 FirstGlance]. <br>
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|ACTIVITY=
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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]] 3.4&#8491;</td></tr>
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|GENE= hMtCCA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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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=1ou5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ou5 OCA], [https://pdbe.org/1ou5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ou5 RCSB], [https://www.ebi.ac.uk/pdbsum/1ou5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ou5 ProSAT]</span></td></tr>
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|DOMAIN=
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</table>
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|RELATEDENTRY=[[1miv|1MIV]], [[1miw|1MIW]], [[1miy|1MIY]]
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== Function ==
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ou5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ou5 OCA], [http://www.ebi.ac.uk/pdbsum/1ou5 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ou5 RCSB]</span>
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[https://www.uniprot.org/uniprot/TRNT1_HUMAN TRNT1_HUMAN] Isoform 1: Adds and repairs the conserved 3'-CCA sequence necessary for the attachment of amino acids to the 3' terminus of tRNA molecules, using CTP and ATP as substrates.<ref>PMID:17204286</ref> Isoform 2: Adds 2 C residues (CC-) to the 3' terminus of tRNA molecules instead of a complete CCA end as isoform 1 does (in vitro).<ref>PMID:17204286</ref>
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}}
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ou/1ou5_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1ou5 ConSurf].
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<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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All tRNA molecules carry the invariant sequence CCA at their 3'-terminus for amino acid attachment. The post-transcriptional addition of CCA is carried out by ATP(CTP):tRNA nucleotidyltransferase, also called CCase. This enzyme catalyses a unique template-independent but sequence-specific nucleotide polymerization reaction. In order to reveal the molecular mechanism of this activity, we solved the crystal structure of human CCase by single isomorphous replacement. The structure reveals a four domain architecture with a cluster of conserved residues forming a positively charged cleft between the first two domains. Structural homology of the N-terminal CCase domain to other nucleotidyltransferases could be exploited for modeling a tRNA-substrate complex. The model places the tRNA 3'-end into the N-terminal nucleotidyltransferase site, close to a patch of conserved residues that provide the binding sites for CTP and ATP. Based on our results, we introduce a corkscrew model for CCA addition that includes a fixed active site and a traveling tRNA-binding region formed by flexible parts of the protein.
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'''Crystal structure of human CCA-adding enzyme'''
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Crystal structure of the human CCA-adding enzyme: insights into template-independent polymerization.,Augustin MA, Reichert AS, Betat H, Huber R, Morl M, Steegborn C J Mol Biol. 2003 May 16;328(5):985-94. PMID:12729736<ref>PMID:12729736</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 1ou5" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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All tRNA molecules carry the invariant sequence CCA at their 3'-terminus for amino acid attachment. The post-transcriptional addition of CCA is carried out by ATP(CTP):tRNA nucleotidyltransferase, also called CCase. This enzyme catalyses a unique template-independent but sequence-specific nucleotide polymerization reaction. In order to reveal the molecular mechanism of this activity, we solved the crystal structure of human CCase by single isomorphous replacement. The structure reveals a four domain architecture with a cluster of conserved residues forming a positively charged cleft between the first two domains. Structural homology of the N-terminal CCase domain to other nucleotidyltransferases could be exploited for modeling a tRNA-substrate complex. The model places the tRNA 3'-end into the N-terminal nucleotidyltransferase site, close to a patch of conserved residues that provide the binding sites for CTP and ATP. Based on our results, we introduce a corkscrew model for CCA addition that includes a fixed active site and a traveling tRNA-binding region formed by flexible parts of the protein.
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*[[CCA-adding enzyme 3D structures|CCA-adding enzyme 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1OU5 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OU5 OCA].
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__TOC__
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</StructureSection>
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==Reference==
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Crystal structure of the human CCA-adding enzyme: insights into template-independent polymerization., Augustin MA, Reichert AS, Betat H, Huber R, Morl M, Steegborn C, J Mol Biol. 2003 May 16;328(5):985-94. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12729736 12729736]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Augustin, M A.]]
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[[Category: Augustin MA]]
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[[Category: Betat, H.]]
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[[Category: Betat H]]
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[[Category: Huber, R.]]
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[[Category: Huber R]]
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[[Category: Moerl, M.]]
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[[Category: Moerl M]]
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[[Category: Reichert, A S.]]
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[[Category: Reichert AS]]
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[[Category: Steegborn, C.]]
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[[Category: Steegborn C]]
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[[Category: nucleotidyltransferase]]
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[[Category: polymerase]]
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[[Category: trna]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:50:21 2008''
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Current revision

Crystal structure of human CCA-adding enzyme

PDB ID 1ou5

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