5mkp
From Proteopedia
(Difference between revisions)
m (Protected "5mkp" [edit=sysop:move=sysop]) |
|||
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==Non redox thiolation in transfer RNAs occuring via sulfur activation by a [4Fe-4S] cluster== | |
| + | <StructureSection load='5mkp' size='340' side='right' caption='[[5mkp]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5mkp]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MKP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5MKP FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=Q46:Fe4+H+S5'>Q46</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3vrh|3vrh]]</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=5mkp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mkp OCA], [http://pdbe.org/5mkp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5mkp RCSB], [http://www.ebi.ac.uk/pdbsum/5mkp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5mkp ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Sulfur is present in several nucleosides within tRNAs. In particular, thiolation of the universally conserved methyl-uridine at position 54 stabilizes tRNAs from thermophilic bacteria and hyperthermophilic archaea and is required for growth at high temperature. The simple nonredox substitution of the C2-uridine carbonyl oxygen by sulfur is catalyzed by tRNA thiouridine synthetases called TtuA. Spectroscopic, enzymatic, and structural studies indicate that TtuA carries a catalytically essential [4Fe-4S] cluster and requires ATP for activity. A series of crystal structures shows that (i) the cluster is ligated by only three cysteines that are fully conserved, allowing the fourth unique iron to bind a small ligand, such as exogenous sulfide, and (ii) the ATP binding site, localized thanks to a protein-bound AMP molecule, a reaction product, is adjacent to the cluster. A mechanism for tRNA sulfuration is suggested, in which the unique iron of the catalytic cluster serves to bind exogenous sulfide, thus acting as a sulfur carrier. | ||
| - | + | Nonredox thiolation in tRNA occurring via sulfur activation by a [4Fe-4S] cluster.,Arragain S, Bimai O, Legrand P, Caillat S, Ravanat JL, Touati N, Binet L, Atta M, Fontecave M, Golinelli-Pimpaneau B Proc Natl Acad Sci U S A. 2017 Jul 11;114(28):7355-7360. doi:, 10.1073/pnas.1700902114. Epub 2017 Jun 27. PMID:28655838<ref>PMID:28655838</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5mkp" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Arragain, S]] | ||
| + | [[Category: Bimai, O]] | ||
| + | [[Category: Golinelli-Pimpaneau, B]] | ||
| + | [[Category: Legrand, P]] | ||
| + | [[Category: Iron-sulfur cluster]] | ||
| + | [[Category: Rna]] | ||
| + | [[Category: Sulfur insertion]] | ||
| + | [[Category: Thiolation reaction]] | ||
| + | [[Category: Trna modification]] | ||
| + | [[Category: Ttua]] | ||
Revision as of 10:38, 3 August 2017
Non redox thiolation in transfer RNAs occuring via sulfur activation by a [4Fe-4S] cluster
| |||||||||||
