View source for 4jc0


==Crystal structure of Thermotoga maritima holo RimO in complex with pentasulfide, Northeast Structural Genomics Consortium Target VR77==
<StructureSection load='4jc0' size='340' side='right'caption='[[4jc0]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4jc0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JC0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JC0 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.3&#8491;</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=4jc0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jc0 OCA], [https://pdbe.org/4jc0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4jc0 RCSB], [https://www.ebi.ac.uk/pdbsum/4jc0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4jc0 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RIMO_THEMA RIMO_THEMA] Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein S12 (By similarity).
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
How living organisms create carbon-sulfur bonds during the biosynthesis of critical sulfur-containing compounds is still poorly understood. The methylthiotransferases MiaB and RimO catalyze sulfur insertion into tRNAs and ribosomal protein S12, respectively. Both belong to a subgroup of radical-S-adenosylmethionine (radical-SAM) enzymes that bear two [4Fe-4S] clusters. One cluster binds S-adenosylmethionine and generates an Ado* radical via a well-established mechanism. However, the precise role of the second cluster is unclear. For some sulfur-inserting radical-SAM enzymes, this cluster has been proposed to act as a sacrificial source of sulfur for the reaction. In this paper, we report parallel enzymological, spectroscopic and crystallographic investigations of RimO and MiaB, which provide what is to our knowledge the first evidence that these enzymes are true catalysts and support a new sulfation mechanism involving activation of an exogenous sulfur cosubstrate at an exchangeable coordination site on the second cluster, which remains intact during the reaction.

Two Fe-S clusters catalyze sulfur insertion by radical-SAM methylthiotransferases.,Forouhar F, Arragain S, Atta M, Gambarelli S, Mouesca JM, Hussain M, Xiao R, Kieffer-Jaquinod S, Seetharaman J, Acton TB, Montelione GT, Mulliez E, Hunt JF, Fontecave M Nat Chem Biol. 2013 Mar 31. doi: 10.1038/nchembio.1229. PMID:23542644<ref>PMID:23542644</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4jc0" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Thermotoga maritima]]
[[Category: Acton TB]]
[[Category: Chen CX]]
[[Category: Conover K]]
[[Category: Cunningham K]]
[[Category: Fang Y]]
[[Category: Forouhar F]]
[[Category: Hunt JF]]
[[Category: Hussain M]]
[[Category: Ma L-C]]
[[Category: Montelione GT]]
[[Category: Seetharaman J]]
[[Category: Tong L]]
[[Category: Xiao R]]