4JC0

Crystal structure of Thermotoga maritima holo RimO in complex with pentasulfide, Northeast Structural Genomics Consortium Target VR77

Summary for 4JC0

• Entry DOI: 10.2210/pdb4jc0/pdb
• Descriptor: Ribosomal protein S12 methylthiotransferase RimO, IRON/SULFUR PENTA-SULFIDE CONNECTED CLUSTERS (2 entities in total)
• Functional Keywords: structural genomics, psi-biology, northeast structural genomics consortium, nesg, three-domained enzyme, alpha-beta n-terminal domain, semi-tim barrel radical-sam domain, beta barrel c-terminal tram domain, ribosomal protein s12, transferase
• Biological source: Thermotoga maritima
• Cellular location: Cytoplasm (Potential): Q9X2H6
• Total number of polymer chains: 2
• Total formula weight: 102447.92

Authors

Forouhar, F.,Hussain, M.,Seetharaman, J.,Fang, Y.,Chen, C.X.,Cunningham, K.,Conover, K.,Ma, L.-C.,Xiao, R.,Acton, T.B.,Montelione, G.T.,Tong, L.,Hunt, J.F.,Northeast Structural Genomics Consortium (NESG) (deposition date: 2013-02-20, release date: 2013-04-10, Last modification date: 2023-09-20)

Primary citation

Forouhar, F.,Arragain, S.,Atta, M.,Gambarelli, S.,Mouesca, J.M.,Hussain, M.,Xiao, R.,Kieffer-Jaquinod, S.,Seetharaman, J.,Acton, T.B.,Montelione, G.T.,Mulliez, E.,Hunt, J.F.,Fontecave, M.
Two Fe-S clusters catalyze sulfur insertion by radical-SAM methylthiotransferases.
Nat.Chem.Biol., 9:333-338, 2013

PubMed Abstract: 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.

PubMed: 23542644
DOI: 10.1038/nchembio.1229

Experimental method

X-RAY DIFFRACTION (3.3 Å)