5mko: Difference between revisions
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The | ==[2Fe-2S] cluster containing TtuA in complex with AMP.== | ||
<StructureSection load='5mko' size='340' side='right' caption='[[5mko]], [[Resolution|resolution]] 2.65Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5mko]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MKO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5MKO FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</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=5mko FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mko OCA], [http://pdbe.org/5mko PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5mko RCSB], [http://www.ebi.ac.uk/pdbsum/5mko PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5mko 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 5mko" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Arragain, S]] | |||
[[Category: Bimai, O]] | |||
[[Category: Golinelli-Pimpaneau, B]] | |||
[[Category: Legrand, P]] | |||
[[Category: 2fe-2]] | |||
[[Category: Amp]] | |||
[[Category: Iron-sulfur cluster]] | |||
[[Category: Ph0300]] | |||
[[Category: Rna]] | |||
[[Category: Thiolation]] | |||
[[Category: Trna modification enzyme]] | |||
[[Category: Ttua]] | |||
Revision as of 11:13, 3 August 2017
[2Fe-2S] cluster containing TtuA in complex with AMP.[2Fe-2S] cluster containing TtuA in complex with AMP.
Structural highlights
Publication Abstract from PubMedSulfur 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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