4jc0
From Proteopedia
(Difference between revisions)
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| - | + | ==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]] 3.30Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[4jc0]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4JC0 FirstGlance]. <br> | |
| - | ==Function== | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FS5:IRON/SULFUR+PENTA-SULFIDE+CONNECTED+CLUSTERS'>FS5</scene></td></tr> |
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rimO, TM1862, TM_1862 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 Thermotoga maritima])</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=4jc0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jc0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4jc0 RCSB], [http://www.ebi.ac.uk/pdbsum/4jc0 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
[[http://www.uniprot.org/uniprot/RIMO_THEMA RIMO_THEMA]] Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein S12 (By similarity). | [[http://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®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Thermotoga maritima]] | [[Category: Thermotoga maritima]] | ||
| - | [[Category: Acton, T B | + | [[Category: Acton, T B]] |
| - | [[Category: Chen, C X | + | [[Category: Chen, C X]] |
| - | [[Category: Conover, K | + | [[Category: Conover, K]] |
| - | [[Category: Cunningham, K | + | [[Category: Cunningham, K]] |
| - | [[Category: Fang, Y | + | [[Category: Fang, Y]] |
| - | [[Category: Forouhar, F | + | [[Category: Forouhar, F]] |
| - | [[Category: Hunt, J F | + | [[Category: Hunt, J F]] |
| - | [[Category: Hussain, M | + | [[Category: Hussain, M]] |
| - | [[Category: Ma, L C | + | [[Category: Ma, L C]] |
| - | [[Category: Montelione, G T | + | [[Category: Montelione, G T]] |
| - | [[Category: | + | [[Category: Structural genomic]] |
| - | [[Category: Seetharaman, J | + | [[Category: Seetharaman, J]] |
| - | [[Category: Tong, L | + | [[Category: Tong, L]] |
| - | [[Category: Xiao, R | + | [[Category: Xiao, R]] |
[[Category: Alpha-beta n-terminal domain]] | [[Category: Alpha-beta n-terminal domain]] | ||
[[Category: Beta barrel c-terminal tram domain]] | [[Category: Beta barrel c-terminal tram domain]] | ||
[[Category: Nesg]] | [[Category: Nesg]] | ||
| - | [[Category: Northeast structural genomics consortium]] | ||
[[Category: Psi-biology]] | [[Category: Psi-biology]] | ||
[[Category: Ribosomal protein s12]] | [[Category: Ribosomal protein s12]] | ||
[[Category: Semi-tim barrel radical-sam domain]] | [[Category: Semi-tim barrel radical-sam domain]] | ||
| - | [[Category: Structural genomic]] | ||
[[Category: Three-domained enzyme]] | [[Category: Three-domained enzyme]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
Revision as of 22:02, 25 December 2014
Crystal structure of Thermotoga maritima holo RimO in complex with pentasulfide, Northeast Structural Genomics Consortium Target VR77
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Categories: Thermotoga maritima | Acton, T B | Chen, C X | Conover, K | Cunningham, K | Fang, Y | Forouhar, F | Hunt, J F | Hussain, M | Ma, L C | Montelione, G T | Structural genomic | Seetharaman, J | Tong, L | Xiao, R | Alpha-beta n-terminal domain | Beta barrel c-terminal tram domain | Nesg | Psi-biology | Ribosomal protein s12 | Semi-tim barrel radical-sam domain | Three-domained enzyme | Transferase
