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 degrees 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].
Julien
Olivier
O
Département de biochimie et de microbiologie and CREFSIP, Université Laval, 3255 pav. Marchand, Québec, G1K 7P4, Canada.
Gignac
Isabelle
I
Hutton
Anna
A
Yee
Adelinda
A
Arrowsmith
Cheryl H
CH
Gagné
Stéphane M
SM
D019843:Archaeal Proteins / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy; D017014:Methanobacterium / Q000737:chemistry*; D008958:Models, Molecular; D011487:Protein Conformation; D020449:Repetitive Sequences, Amino Acid
D019843:Archaeal Proteins