MTH187 from Methanobacterium thermoautotrophicum has three HEAT-like Repeats

With the completion of genome sequencing projects, there are a large number of proteins for which we have little or no functional information. Since protein function is closely related to three-dimensional conformation, structural proteomics is one avenue where the role of proteins with unknown function can be investigated. In the present structural project, the structure of MTH187 has been determined by solution-state NMR spectroscopy. This protein of 12.4 kDa is one of the 424 non-membrane proteins that were cloned and purified for the structural proteomic project of Methanobacterium thermoautotrophicum Christendat, D., Yee, A., Dharamsi, A., Kluger, Y., Gerstein, M., Arrowsmith, C.H. and Edwards, A.M. (2000) Prog. Biophys. Mol. Biol., 73, 339–345]. Methanobacterium thermoautotrophicum is a thermophilic archaeon that grows optimally at 65 °C. A particular characteristic of this microorganism is its ability to generate methane from carbon dioxide and hydrogen Smith, D.R., Doucette-Stamm, L.A., Deloughery, C., Lee, H., Dubois, J., Aldredge, T., Bashirzadeh, R., Blakely, D., Cook, R., Gilbert, K., Harrison, D., Hoang, L., Keagle, P., Lumm, W., Pothier, B., Qiu, D., Spadafora, R., Vicaire, R., Wang, Y., Wierzbowski, J., Gibson, R., Jiwani, N., Caruso, A., Bush, D., Reeve, J. N. et al. (1997) J. Bacteriol., 179, 7135–7155].Electronic supplementary material Electronic supplementary material is available for this article at and accessible for authorised users. Structure data have been deposited at PDB (1TE4) and NMR data at BMRB (5629).Olivier Julien and Isabelle Gignac - Both authors contributed equally to this work.