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4x4v

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Revision as of 00:23, 26 January 2017

Crystal structure of the A.fulgidus CCA-adding enzyme in complex with a human MenBeta minihelix ending in CCACC and AMPcPP

Structural highlights

4x4v is a 4 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , , ,
Related:	4x4n, 4x4o, 4x4p, 4x4q, 4x4r, 4x4s, 4x4t, 4x4u, 4x4w, 4x4x
Activity:	CCA tRNA nucleotidyltransferase, with EC number 2.7.7.72
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.^[1]

Publication Abstract from PubMed

Transcription in eukaryotes produces a number of long noncoding RNAs (lncRNAs). Two of these, MALAT1 and Menbeta, generate a tRNA-like small RNA in addition to the mature lncRNA. The stability of these tRNA-like small RNAs and bona fide tRNAs is monitored by the CCA-adding enzyme. Whereas CCA is added to stable tRNAs and tRNA-like transcripts, a second CCA repeat is added to certain unstable transcripts to initiate their degradation. Here, we characterize how these two scenarios are distinguished. Following the first CCA addition cycle, nucleotide binding to the active site triggers a clockwise screw motion, producing torque on the RNA. This ejects stable RNAs, whereas unstable RNAs are refolded while bound to the enzyme and subjected to a second CCA catalytic cycle. Intriguingly, with the CCA-adding enzyme acting as a molecular vise, the RNAs proofread themselves through differential responses to its interrogation between stable and unstable substrates.

On-Enzyme Refolding Permits Small RNA and tRNA Surveillance by the CCA-Adding Enzyme.,Kuhn CD, Wilusz JE, Zheng Y, Beal PA, Joshua-Tor L Cell. 2015 Feb 12;160(4):644-58. doi: 10.1016/j.cell.2015.01.005. Epub 2015 Jan, 29. PMID:25640237^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Okabe M, Tomita K, Ishitani R, Ishii R, Takeuchi N, Arisaka F, Nureki O, Yokoyama S. Divergent evolutions of trinucleotide polymerization revealed by an archaeal CCA-adding enzyme structure. EMBO J. 2003 Nov 3;22(21):5918-27. PMID:14592988 doi:http://dx.doi.org/10.1093/emboj/cdg563
↑ Kuhn CD, Wilusz JE, Zheng Y, Beal PA, Joshua-Tor L. On-Enzyme Refolding Permits Small RNA and tRNA Surveillance by the CCA-Adding Enzyme. Cell. 2015 Feb 12;160(4):644-58. doi: 10.1016/j.cell.2015.01.005. Epub 2015 Jan, 29. PMID:25640237 doi:http://dx.doi.org/10.1016/j.cell.2015.01.005

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4x4v"

@@ Line 1: / Line 1: @@
 ==Crystal structure of the A.fulgidus CCA-adding enzyme in complex with a human MenBeta minihelix ending in CCACC and AMPcPP==
 <StructureSection load='4x4v' size='340' side='right' caption='[[4x4v]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4x4n|4x4n]], [[4x4o|4x4o]], [[4x4p|4x4p]], [[4x4q|4x4q]], [[4x4r|4x4r]], [[4x4s|4x4s]], [[4x4t|4x4t]], [[4x4u|4x4u]], [[4x4w|4x4w]], [[4x4x|4x4x]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/CCA_tRNA_nucleotidyltransferase CCA tRNA nucleotidyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.72 2.7.7.72] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4x4v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x4v OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4x4v RCSB], [http://www.ebi.ac.uk/pdbsum/4x4v PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4x4v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x4v OCA], [http://pdbe.org/4x4v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4x4v RCSB], [http://www.ebi.ac.uk/pdbsum/4x4v PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4x4v ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 18: / Line 19: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4x4v" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[CCA-adding enzyme|CCA-adding enzyme]]
+*[[TRNA|TRNA]]
 == References ==
 <references/>

4x4v

From Proteopedia

Revision as of 00:23, 26 January 2017

Crystal structure of the A.fulgidus CCA-adding enzyme in complex with a human MenBeta minihelix ending in CCACC and AMPcPP

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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