1ou5

<table><tr><td colspan='2'>[[1ou5]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. 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 [http://proteopedia.org/fgij/fg.htm?mol=1OU5 FirstGlance]. <br>

</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1miv|1miv]], [[1miw|1miw]], [[1miy|1miy]]</div></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hMtCCA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1ou5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ou5 OCA], [http://pdbe.org/1ou5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ou5 RCSB], [http://www.ebi.ac.uk/pdbsum/1ou5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ou5 ProSAT]</span></td></tr>

[[http://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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== Publication Abstract from PubMed ==

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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1ou5" style="background-color:#fffaf0;"></div>

[[Category: Human]]

[[Category: Augustin, M A]]

[[Category: Betat, H]]

[[Category: Huber, R]]

[[Category: Moerl, M]]

[[Category: Reichert, A S]]

[[Category: Steegborn, C]]

[[Category: Trna]]