2QGQ

Crystal structure of TM_1862 from Thermotoga maritima. Northeast Structural Genomics Consortium target VR77

Summary for 2QGQ

• Entry DOI: 10.2210/pdb2qgq/pdb
• Descriptor: Protein TM_1862, 3-CYCLOHEXYL-1-PROPYLSULFONIC ACID (3 entities in total)
• Functional Keywords: alpha-beta protein, structural genomics, psi-2, protein structure initiative, northeast structural genomics consortium, nesg, unknown function
• Biological source: Thermotoga maritima MSB8
• Cellular location: Cytoplasm : Q9X2H6
• Total number of polymer chains: 8
• Total formula weight: 284561.80

Authors

Forouhar, F.,Neely, H.,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: 2007-06-29, release date: 2007-07-17, Last modification date: 2024-10-16)

Primary citation

Arragain, S.,Garcia-Serres, R.,Blondin, G.,Douki, T.,Clemancey, M.,Latour, J.M.,Forouhar, F.,Neely, H.,Montelione, G.T.,Hunt, J.F.,Mulliez, E.,Fontecave, M.,Atta, M.
Post-translational Modification of Ribosomal Proteins: STRUCTURAL AND FUNCTIONAL CHARACTERIZATION OF RimO FROM THERMOTOGA MARITIMA, A RADICAL S-ADENOSYLMETHIONINE METHYLTHIOTRANSFERASE.
J.Biol.Chem., 285:5792-5801, 2010

PubMed Abstract: Post-translational modifications of ribosomal proteins are important for the accuracy of the decoding machinery. A recent in vivo study has shown that the rimO gene is involved in generation of the 3-methylthio derivative of residue Asp-89 in ribosomal protein S12 (Anton, B. P., Saleh, L., Benner, J. S., Raleigh, E. A., Kasif, S., and Roberts, R. J. (2008) Proc. Natl. Acad. Sci. U. S. A. 105, 1826-1831). This reaction is formally identical to that catalyzed by MiaB on the C2 of adenosine 37 near the anticodon of several tRNAs. We present spectroscopic evidence that Thermotoga maritima RimO, like MiaB, contains two [4Fe-4S] centers, one presumably bound to three invariant cysteines in the central radical S-adenosylmethionine (AdoMet) domain and the other to three invariant cysteines in the N-terminal UPF0004 domain. We demonstrate that holo-RimO can specifically methylthiolate the aspartate residue of a 20-mer peptide derived from S12, yielding a mixture of mono- and bismethylthio derivatives. Finally, we present the 2.0 A crystal structure of the central radical AdoMet and the C-terminal TRAM (tRNA methyltransferase 2 and MiaB) domains in apo-RimO. Although the core of the open triose-phosphate isomerase (TIM) barrel of the radical AdoMet domain was conserved, RimO showed differences in domain organization compared with other radical AdoMet enzymes. The unusually acidic TRAM domain, likely to bind the basic S12 protein, is located at the distal edge of the radical AdoMet domain. The basic S12 protein substrate is likely to bind RimO through interactions with both the TRAM domain and the concave surface of the incomplete TIM barrel. These biophysical results provide a foundation for understanding the mechanism of methylthioation by radical AdoMet enzymes in the MiaB/RimO family.

PubMed: 20007320
DOI: 10.1074/jbc.M109.065516

Experimental method

X-RAY DIFFRACTION (2 Å)