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| <StructureSection load='2nr0' size='340' side='right'caption='[[2nr0]], [[Resolution|resolution]] 3.90Å' scene=''> | | <StructureSection load='2nr0' size='340' side='right'caption='[[2nr0]], [[Resolution|resolution]] 3.90Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[2nr0]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NR0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NR0 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2nr0]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NR0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NR0 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;'>[[1dj0|1dj0]], [[2nqp|2nqp]], [[2nre|2nre]]</div></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.9Å</td></tr> |
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">truA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>
| + | |
- | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/tRNA_pseudouridine(38-40)_synthase tRNA pseudouridine(38-40) synthase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.99.12 5.4.99.12] </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=2nr0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nr0 OCA], [https://pdbe.org/2nr0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2nr0 RCSB], [https://www.ebi.ac.uk/pdbsum/2nr0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2nr0 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=2nr0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nr0 OCA], [https://pdbe.org/2nr0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2nr0 RCSB], [https://www.ebi.ac.uk/pdbsum/2nr0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2nr0 ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Function == | | == Function == |
- | [[https://www.uniprot.org/uniprot/TRUA_ECOLI TRUA_ECOLI]] Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.<ref>PMID:17466622</ref>
| + | [https://www.uniprot.org/uniprot/TRUA_ECOLI TRUA_ECOLI] Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.<ref>PMID:17466622</ref> |
| == Evolutionary Conservation == | | == Evolutionary Conservation == |
| [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Ecoli]] | + | [[Category: Escherichia coli]] |
| + | [[Category: Escherichia coli K-12]] |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Hur, S]] | + | [[Category: Hur S]] |
- | [[Category: Stroud, R M]] | + | [[Category: Stroud RM]] |
- | [[Category: Anticodon stem loop]]
| + | |
- | [[Category: Isomerase-rna complex]]
| + | |
- | [[Category: Multisite specificity]]
| + | |
- | [[Category: Pseudouridine synthase]]
| + | |
- | [[Category: Trna]]
| + | |
| Structural highlights
Function
TRUA_ECOLI Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Translational accuracy and efficiency depend upon modification of uridines in the tRNA anticodon stem loop (ASL) by a highly conserved pseudouridine synthase TruA. TruA specifically modifies uridines at positions 38, 39, and/or 40 of tRNAs with highly divergent sequences and structures through a poorly characterized mechanism that differs from previously studied RNA-modifying enzymes. The molecular basis for the site and substrate "promiscuity" was studied by determining the crystal structures of E. coli TruA in complex with two different leucyl tRNAs in conjunction with functional assays and computer simulation. The structures capture three stages of the TruA*tRNA reaction, revealing the mechanism by which TruA selects the target site. We propose that TruA utilizes the intrinsic flexibility of the ASL for site promiscuity and also to select against intrinsically stable tRNAs to avoid their overstabilization through pseudouridylation, thereby maintaining the balance between the flexibility and stability required for its biological function.
How U38, 39, and 40 of many tRNAs become the targets for pseudouridylation by TruA.,Hur S, Stroud RM Mol Cell. 2007 Apr 27;26(2):189-203. PMID:17466622[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Hur S, Stroud RM. How U38, 39, and 40 of many tRNAs become the targets for pseudouridylation by TruA. Mol Cell. 2007 Apr 27;26(2):189-203. PMID:17466622 doi:10.1016/j.molcel.2007.02.027
- ↑ Hur S, Stroud RM. How U38, 39, and 40 of many tRNAs become the targets for pseudouridylation by TruA. Mol Cell. 2007 Apr 27;26(2):189-203. PMID:17466622 doi:10.1016/j.molcel.2007.02.027
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