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5mkp

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'''Unreleased structure'''
 
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The entry 5mkp is ON HOLD
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==Non redox thiolation in transfer RNAs occuring via sulfur activation by a [4Fe-4S] cluster==
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<StructureSection load='5mkp' size='340' side='right' caption='[[5mkp]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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== Structural highlights ==
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<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>
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</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>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3vrh|3vrh]]</td></tr>
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<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>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Authors:
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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>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 5mkp" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Arragain, S]]
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[[Category: Bimai, O]]
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[[Category: Golinelli-Pimpaneau, B]]
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[[Category: Legrand, P]]
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[[Category: Iron-sulfur cluster]]
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[[Category: Rna]]
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[[Category: Sulfur insertion]]
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[[Category: Thiolation reaction]]
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[[Category: Trna modification]]
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[[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

5mkp, resolution 2.50Å

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